Use of streptococcus pneumoniae acyl carrier protein synthase crystal structure in diagnostics, antimicrobial drug design, and biosensors

ABSTRACT

Provided are methods of purifying and crystallizing  Streptococcus pneumoniae  acyl carrier protein synthase (AcpS) enzyme, crystals of AcpS, the use of such crystals to determine the three-dimensional structure of AcpS enzymes, and the three-dimensional structure of AcpS. The three-dimensional crystal structure of AcpS can be used in medical diagnostics to produce antibodies that permit detection of  Streptococcus pneumoniae  both in vitro and in vivo. The three-dimensional crystal structure of AcpS can also be used in pharmaceutical discovery and development to identify and design compounds that inhibit the biochemical activity of AcpS enzyme in bacteria. Inhibitory compounds identified in this way can be optimized by structure/activity studies to develop antibacterial pharmaceutical compounds useful for the prevention or treatment of bacterial infections.

[0001] This application claims the benefit of priority of U.S.Provisional Patent Application Serial No. 60/215,577 filed on Jun. 30,2000, the contents of which are herein incorporated by reference intheir entirety.

BACKGROUND OF THE INVENTION

[0002] 1. Field of the Invention

[0003] The present invention relates to the fields of proteincrystallography, medical diagnostics, and pharmaceutical development.More particularly, the present invention relates to methods of purifyingand crystallizing Streptococcus pneumoniae acyl carrier protein synthase(AcpS) enzyme, crystals of AcpS enzyme, the use of these crystals todetermine the three-dimensional structure of AcpS enzyme, and to thethree-dimensional structure of AcpS enzyme. The three-dimensionalcrystal structure of the AcpS enzyme can be used in medical diagnosticsto produce antibodies that permit detection of Streptococcus pneumoniaeboth in vitro and in vivo, and therefore accurate diagnosis ofinfections caused by this bacterium. The three-dimensional crystalstructure of AcpS can also be used in pharmaceutical discovery anddevelopment to identify and design compounds that inhibit thebiochemical activity of AcpS enzyme in bacteria. The inhibitory activityof compounds identified in this way can be optimized bystructure/activity studies to develop antibacterial pharmaceuticalcompounds for the prevention or treatment of bacterial infections inmammals.

[0004] 2. Description of Related Art

[0005] Bacterial Drug Resistance

[0006] The emerging resistance of bacteria to antibiotics is afrightening clinical problem (Cohen, 1992; Neu, 1992; Davies, 1994;Spratt, 1994a). A number of common pathogenic bacterial species such asStreptococcus pneumoniae, Staphylococcus aureus, Enterococcus, Shigelladysenteriae, and Mycobacterium tuberculosis have developed resistance toalmost all of the antibiotics, including β-lactams and quinolones, twoof the largest and most important classes of antibiotics that have beenwidely prescribed for upper respiratory tract infections (Cohen, 1992;Neu, 1992; Davies, 1994; Spratt, 1994b; Tomasz and Munoz, 1995; Thomsonand Sanders, 1998; Ahamed et al., 1999). The β-lactam and quinoloneantibiotics are known to target the biosynthesis of bacterial cell wallsand DNA replication, respectively (Neu, 1992; Davies, 1994; Spratt,1994b; Tomasz and Munoz, 1995 Thomson and Sanders, 1998).

[0007] Bacterial Acyl Carrier Protein Synthases

[0008] The biosynthesis of fatty acids is known to be required for thegrowth of bacteria as fatty acids are essential components of bacterialmembrane lipids and lipopoly-saccharides (Cronan and Rock, 1996; Rockand Cronan, 1996). The fatty acid biosynthetic pathway in bacteria iswell characterized (Cronan and Rock, 1996; Rock and Cronan, 1996).Bacteria utilize the type II, or dissociated fatty acid synthase system,for fatty acid synthesis (Cronan and Rock, 1996; Rock and Cronan, 1996).The type II fatty acid synthase system consists of individual enzymesthat are encoded by separate genes (Cronan and Rock, 1996; Rock andCronan, 1996). On the other hand, the type I fatty acid synthase system,almost exclusively present in eukaryotes, is characterized by thepresence of a multifunctional protein that possesses all the catalyticactivities required for fatty acid synthesis (S. Smith, 1994). In bothsystems, fatty acids are synthesized by using a repeated cycle ofcondensation, reduction, dehydration, and reduction reactions (Cronanand Rock, 1996; Rock and Cronan, 1996; S. Smith, 1994). In thesereactions, holo-acyl carrier protein (holo-ACP) plays an essential roleas an acyl carrier for fatty acid precursors, growing acylintermediates, and nascent fatty acid products (Cronan and Rock, 1996;Rock and Cronan, 1996; S. Smith, 1994; Elovson and Vagelos, 1968;Lambalot and Walsh, 1995).

[0009] ACP is a small acidic protein in bacteria (Cronan and Rock, 1996;Rock and Cronan, 1996) or a small domain of the type I fatty acidsynthase in eukaryotes (S. Smith, 1994). ACP in E. coli is encoded bythe acpP gene (Cronan and Rock, 1996; Rock and Cronan, 1996). The newlysynthesized ACP, or apo-ACP, is not functional in fatty acid synthesis.The conversion of apo-ACP to holo-ACP, by ACP synthase (AcpS) isrequired for its functionality (Cronan and Rock, 1996; Rock and Cronan,1996; Elovson and Vagelos, 1968; Lambalot and Walsh, 1995). Theenzymatic step of the reaction that converts apo-acyl carrier protein(apo-ACP) to holo-ACP (Elovson and Vagelos, 1968; Lam et al., 1992;Lambalot and Walsh, 1995; Lambalot et al., 1996; McAllister et al.,2000) is catalyzed by ACP synthase (AcpS), encoded by the acpS gene.This reaction involves the transfer of the 4′-phosphopantetheine groupof Coenzyme A (CoA) onto a serine residue of apo-ACP, thereby convertingapo-ACP to holo-ACP (Elovson and Vagelos, 1968; Lam et al., 1992;Lambalot and Walsh, 1995; Lambalot et al., 1996). The resulting holo-ACPmediates the transfer of fatty acid intermediates during thebiosynthesis of fatty acids and lipids via the covalent attachment ofcarboxyl groups of fatty acid intermediates to the thiol of the4′-phosphopantetheine prosthetic group of holo-ACP (Elovson and Vagelos,1968; Lam et al., 1992; Magnuson et al., 1993; Lambalot and Walsh, 1995;Lambalot et al., 1996). This reaction is therefore required for thebiosynthesis of all bacterial fatty acids, lipid A, which is anessential component of bacterial lipopolysacchrides, and the membranelipids, which are also derived exclusively from acyl intermediates offatty acids (Magnuson et al., 1993). The essential nature of thisreaction has been well established genetically in E. coli and S.pneumoniae (Lam et al., 1992; Takiff et al., 1992; McAllister et al.,2000). Consistent with its important role in fatty acid biosynthesis,AcpS is widely present in Mycoplasma, as well as gram-negative andgram-positive bacteria. Homologues of AcpS and ACP have been identifiedin many bacterial genomes sequenced to date (Blattner et al., 1997; Coleet al., 1998; Himmelreich et al., 1996; Kalman et al., 1999); Kuns etal., 1997; Tomb et al., 1997). Thus, AcpS appears to be an attractiveantibacterial target for discovery of novel antimicrobial agents.

[0010]E. coli AcpS has been well studied (Majerus et al., 1965; Elovsonand Vagelos, 1968; Lambalot and Walsh, 1995; Lambalot et al., 1996;Gehring et al., 1997; Flugel et al., 2000). The acpS gene from E. coliforms an operon with the upstream gene, pdxJ, whose function is requiredfor vitamin B₆ biosynthesis (Lam et al., 1992; Takiff et al., 1992). TheacpS gene was originally identified as dpj (downstream of pdxJ) whosefunction, although unknown, was required for the growth of E. coli (Lamet al., 1992; Takiff et al., 1992). Later, the landmark biochemicalstudy by Lambalot and Walsh (1995) led to the identification of Dpj asAcpS. E. coli AcpS is a small, highly basic protein of approximately 14kDa (Lambalot and Walsh, 1995). The E. coli enzyme has been purified andcharacterized (Lambalot and Walsh, 1995). The enzyme exhibits a broadsubstrate specificity, and can utilize a variety of AcpS, which arerequired for many diverse aspects of cellular metabolism (Majerus etal., 1965; Crosby et al., 1995; Lambalot and Walsh, 1995; Lambalot etal., 1996; Carreas et al., 1997; Gehring et al., 1997; Tropf et al.,1998; Kutchma et al., 1999; Zhou et al, 1999; Flugel et al., 2000).Purified AcpS also exhibits activity with a number of CoA derivatives(Gehring et al., 1997). These results indicate that AcpS may be able toparticipate in other metabolism besides fatty acid biosynthesis in thecell. Purified AcpS also exhibits activity with a number of CoAderivatives (Gehring et al., 1997). Finally, AcpS is a very lowabundance protein in E. coli (Elovson and Vagelos, 1968; Lamabolt andWalsh, 1995). In contrast, ACP is a very abundant protein that has beenestimated to be present at 25,000-60,000 molecules per cell (Cronan andRock, 1996; Rock and Cronan, 1996; Jackowski and Rock, 1984; Vallari andJackowshi, 1988). The majority of AcpS present in the cell are found tobe holo-AcpS (Cronan and Rock, 1996; Rock and Cronan, 1996; Jackowskiand Rock, 1983; Heath and Rock, 1996).

[0011] Although E. coli AcpS is well studied, the reaction mechanism ofAcpS remains unknown. In addition, only the AcpS from E. coli, arod-shaped, Gram-negative bacterium, has been thoroughly characterizedto date. It still remains to be determined whether AcpS fromGram-positive bacteria plays the same physiological role. Finally, AcpSappears to possess all the features necessary for a good antibacterialtarget, such as its essential nature, widespread existence in bacteria,and unique catalytic position in an important biosynthetic pathway(fatty acid biosynthesis). Thus, AcpS appears to be a valuableantibacterial target for identifying novel antimicrobial agents.

[0012] Recently, AcpS from Streptococcus pneumoniae has been purifiedand characterized (McAllister et al., 2000). The S. pneumoniae enzymeexhibits biochemical properties similar to those of the E. coli AcpS.The acpS gene has also been shown to be essential for the growth of S.pneumoniae (McAllister et al., 2000).

[0013] The crystal structure of Bacillus subtilis AcpS has recently beendescribed by Parris et al. (2000).

[0014] The pressing need for new antibacterial compounds can desirablybe met by methods that do not rely on serendipity and/or systematicscreening of large numbers of natural and synthetic compounds. One suchmethod relies on structure-based drug design using computer modeling andthe three-dimensional crystal structure of bacterial target proteins toidentify and optimize antimicrobial drug candidates. Thethree-dimensional structure of AcpS has heretofore remained unknown asno crystals thereof have been produced that permitted the requiredcrystallographic data to be obtained. Therefore, there is a need in theart for such crystals, for the determination of the three-dimensionalstructure of such crystals, and for structure-based drug design anddiagnostics based on such crystallographic data.

SUMMARY OF THE INVENTION

[0015] Accordingly, in order to exploit bacterial cellular componentsthat can serve as diagnostic agents and antibacterial targets foridentifying novel antibiotics that can be used to combat the currentcrisis of antibiotic resistance, the present inventors have focusedtheir attention on AcpS. The present invention includes among itsvarious aspects crystals of AcpS enzyme, use of such AcpS crystals todetermine the three-dimensional structure of AcpS enzyme, thethree-dimensional crystal structure of AcpS enzyme, methods of drugdiscovery/design and diagnostics based on the three-dimensional crystalstructure AcpS enzyme, use of crystals of AcpS in biosensors and otherapplications, and methods of purifying and crystallizing AcpS enzyme. Asa first step toward structure-based drug design, the present inventionprovides the crystal structures of S. pneumoniae AcpS and theAcpS/3′,5′-ADP complex at 2.0 and 1.9 Å resolution, respectively.

[0016] More specifically, in a first aspect, the present inventionprovides a composition comprising a crystal of isolated Streptococcuspneumoniae AcpS. Such crystal effectively diffracts X-rays, and permitsthe determination of the atomic coordinates of the AcpS to a resolutionof 2.0 Å or greater. As used herein, the term “greater” refers toresolution of the atomic coordinates to a value lower than 2.0 Å.

[0017] More particularly, the present invention provides a compositioncomprising a crystal of Streptococcus pneumoniae AcpS having the aminoacid sequence shown in SEQ ID NO: 1 wherein methionine is substitutedwith selenomethioinine, wherein said AcpS is a homotrimer, wherein eachprotomer comprises the following structural motifs: (a) a three-strandedanti-parallel β-sheet formed by strands β1, β5, and β4; (b) a longα-helix that packs diagonally against said β-sheet, together withα-helices α1 α2, α3, and α4 of an anti-parallel four helical bundle; and(c) a long, extended loop with a two-strand anti-parallel β-sheetcomprising strands β2 and β3, wherein said structural motifs (a), (b),and (c) are organized such that said long helix α4 runs through saidhomotrimer, and is surrounded by the remainder of said structuralmotifs, as shown in FIGS. 8(B) and 8(C). When the AcpS is in nativeform, i.e., the active site is unoccupied, the crystal belongs toorthorhombic space group P2₁2₁2₁, with unit cell dimensions of a=49.8 Å,b=59.6 Å, and c=114.7 Å, or monoclinic space group C2, with unit celldimensions of a=120.2 Å, b=62.3 Å, c=51.7 Å, and β=98.7°. Such crystalscan have the atomic coordinates shown in Tables 3 and 4. When the AcpSis complexed with 3′,5′-adenosine diphosphate, the crystal belongs tomonoclinic space group C2, with unit cell dimensions of a=120.2 Å,b=62.3 Å, c=51.7 Å, and β=98.7°, and the crystal can have the atomiccoordinates shown in Table 5.

[0018] In another aspect, the present invention provides an enzymeactive site crystal structure comprising the 3′,5′-adenosine diphosphatebinding site shown in FIG. 9. More particularly, the enzyme comprisesisolated, properly folded Streptococcus pneumoniae AcpS, or a fragmentor protein fusion product thereof comprising the active site. Alsoencompassed by the present invention are active site crystal structuresthat are variants or homologs of the AcpS binding pocket having a rootmean square deviation from the amino acid residues comprising the AcpSactive site shown in FIG. 9 in the range of from about 1 to about 3 Å,more preferably from about 1 to about 2 Å, and most preferably of about1.15 Å. Such active sites can form binding complexes with an ACP, a CoA,an apo-ACP, an acetyl-CoA, a desulfo-CoA, an acetoacetyl-CoA, amalonyl-CoA, or a dephospho-CoA.

[0019] In a further aspect, the present invention provides a method ofisolating Streptococcus pneumoniae AcpS, comprising:

[0020] (a) growing Streptococcus pneumoniae in a medium lackingmethionine but containing L-selenomethionine;

[0021] (b) preparing a cell extract of the Streptococcus pneumoniae;

[0022] (c) centrifuging the cell extract to produce a supernatantfraction, and collecting this supernatant fraction;

[0023] (d) chromatographing the supernatant fraction on a cationexchange column in buffer containing dithiothreitol orβ-mercaptoethanol, and collecting fractions containing the Streptococcuspneumoniae AcpS; and

[0024] (e) chromatographing the fractions of step (d) on a gelfiltration column in buffer containing dithiothreitol orβ-mercaptoethanol, and collecting fractions containing the Streptococcuspneumoniae AcpS comprising L-selenomethionine.

[0025] An additional step in this method can comprise chromatographingthe fractions of step (e) on an anion exchange column in buffercontaining dithiothreitol or β-mercapto-ethanol, and collectingfractions containing Streptococcus pneumoniae AcpS.

[0026] In yet another aspect, the present invention provides isolatedStreptococcus pneumoniae acyl carrier protein synthase produced by theforegoing method.

[0027] In another aspect, the present invention provides a method ofproducing a crystal of Streptococcus pneumoniae AcpS that diffractsX-rays, comprising:

[0028] (a) providing Streptococcus pneumoniae AcpS isolated according tothe foregoing method;

[0029] (b) concentrating the AcpS to 8 mg/ml in a solution containing 10mM MgCl₂, 14 mM KCl, and 20 mM Tris-HCl at pH 7.1;

[0030] (c) equilibrating a 4 μl drop of the AcpS in a solutioncomprising a mixture of 1:1, v/v, protein solution/reservoir solutionover a 500 μl reservoir solution comprising 8-15% polyethyleneglycol4000, 200 mM ammonium sulfate, and 100 mM citrate buffer at pH 4.5; and

[0031] (d) growing a crystal of AcpS by vapor diffusion at 294K for 4 to5 days or longer.

[0032] In another aspect, the present invention provides a crystal ofStreptococcus pneumoniae AcpS produced by the foregoing method.

[0033] In a further aspect, the present invention provides a co-crystalof Streptococcus pneumoniae AcpS with a compound, produced by eitherincluding such compound in the protein solution/reservoir solutionduring crystallization, or by contacting a crystal of AcpS and asolution, such as protein or reservoir solution, comprising suchcompound (“soaking” the crystal in a solution of compound), andincubating the resulting mixture to permit the compound to diffuse intothe crystal, thereby producing a complex between AcpS and the compound.The compound can be 3′,5′-adenosine diphosphate. Whatever compound isemployed, a three-dimensional structure of the resulting acyl carrierprotein synthase/compound crystal complex can then be determined.

[0034] In another aspect, the present invention provides a co-crystal ofAcpS produced by the foregoing or similar method.

[0035] In yet other aspects, the present invention provides the use of athree-dimensional crystal or co-crystal structure of AcpS in medicaldiagnostics, biosensors, and pharmaceutical drug discovery and design.The latter enables methods of treating Streptococcal infectionsutilizing compounds that block the biochemical activity of Streptococcuspneumoniae AcpS enzyme, by, for example, determining a three-dimensionalstructure of AcpS enzyme from Streptococcus pneumoniae, utilizing suchthree-dimensional structure to identify/develop a compound that binds toand inhibits the enzyme, and contacting, either in vitro or in vivo,such compound and Streptococcal cells containing the enzyme, therebyinhibiting the biochemical activity of the enzyme and treating orpreventing Streptococcal infections.

[0036] Further scope of the applicability of the present invention willbecome apparent from the detailed description provided below. However,it should be understood that the detailed description and specificexamples, while indicating preferred embodiments of the presentinvention, are given by way of illustration only since various changesand modifications within the spirit and scope of the invention willbecome apparent to those skilled in the art from this detaileddescription.

BRIEF DESCRIPTION OF THE DRAWINGS AND TABLES

[0037] The file of this patent contains at least one drawing and onetable executed in color. Copies of this patent with color drawing(s) andtables will be provided by the Patent and Trademark Office upon requestand payment of the necessary fee.

[0038] The above and other aspects, features, and advantages of thepresent invention will be better understood from the following detaileddescription taken in conjunction with the accompanying drawings, all ofwhich are given by way of illustration only, and are not limitative ofthe present invention, in which:

[0039]FIGS. 1A and 1B show SDS-PAGE analysis of purified S. pneumoniaeAcpS and apo-ACP, respectively, expressed in E. coli, and purified asdescribed in Example 1. The purified AcpS is analyzed by SDS-PAGE (16%Tricine gels) and stained with Coomassie Blue R-250. FIG. 1A: Each lanecontains 5 μg of protein. Lane M: prestained molecular weight markers.Lane 1: Crude extract of E. coli containing overexpressed S. pneumoniaeAcpS. Lane 2: pooled fractions from 15S Source S column; Lane 3: pooledfractions from S-100 Sepharose column. FIG. 1B: Each lane contains 10 μgof protein. Lane M: prestained molecular weight markers. Lane 1: Crudeextract of E. coli containing overexpressed S. pneumoniae ACP. Lane 2:pooled fractions from Source 15Q column; Lane 3: pooled fractions fromS-100 Sepharose column.

[0040]FIG. 2 shows analysis of the native structure of S. pneumoniaeAcpS and apo-ACP by gel filtration column chromatography. Both AcpS andapo-ACP are purified as described in Example 1. Purified AcpS (27 μM)and apo-ACP (100 μM) are subjected to gel filtration column (S-75Sephadex) chromatography, and their molecular weights are determined asdescribed in Example 1. Panel A shows gel filtration columnchromatograph. Peak A contains both AcpS and apo-ACP, and has an elutionvolume of 10.5 ml with an estimated molecular weight of 53 kDa. Peak Bcontains only AcpS, and has an elution volume of 11.5 ml, with anestimated molecular weight of 38 kDa. The arrow C points to the areawhere apo-ACP elutes. Since apo-ACP does not absorb at 280 nm, there isno apparent protein peak observed. Panel B shows SDS-PAGE analysis ofthe column fractions. All relevant fractions collected from Panel A aresubjected to SDS-PAGE analysis. The gels are stained with SYPRO Orange,and analyzed using a FluorImager.

[0041]FIG. 3 shows analysis of the S. pneumoniae AcpS and apo-ACP nativestructures by cross-linking. AcpS and apo-ACP are purified as describedin Example 1. Purified AcpS (163 μM) and apo-ACP (94 μM) are treatedwithout or with 19.5 and 9.4 mM sulfo-EGS, respectively. The resultingAcpS (Panel A) and apo-ACP (Panel B) preparations are analyzed bySDS-PAGE (16% tricine gels). Panel A: Lane 1: the pre-stained molecularweight marker; lane 2: AcpS untreated with sulfo-EGS; and lane 3: AcpStreated with sulfo-EGS. Panel B: Lane 1, the pre-stained molecularweight marker; lane 2: apo-ACP untreated with sulfo-EGS; lane 3: apo-ACPtreated with sulfo-EGS.

[0042]FIG. 4 shows a kinetic analysis of the effect of apo-ACPconcentrations on the AcpS activity of S. pneumoniae. AcpS activity ismeasured using the HPLC method under conditions where the CoAconcentration is fixed at 20 μM and the apo-ACP concentration is variedfrom 0.5 to 100 μM. A: the substrate (apo-ACP) saturation curve of AcpS.B and C: the double reciprocal plots of the initial velocities of theenzyme versus the various apo-ACP concentrations (<5 μM and >15 μM,respectively).

[0043]FIG. 5 shows a kinetic analysis of the effect of CoAconcentrations on the AcpS activity of S. pneumoniae. AcpS activity ismeasured by the HPLC method under conditions where the CoAconcentrations are varied (2.5-600 μM) and the apo-ACP concentration isfixed (2 μM). A: the substrate (CoA) saturation curve of AcpS. B: thedouble reciprocal plot of the initial velocities of AcpS versus CoAconcentrations.

[0044]FIG. 6 shows an analysis of the mechanism of the AcpS catalyzedreaction.

[0045] AcpS activity is measured using HPLC methods. A:double-reciprocal plots of the initial velocities of AcpS versus thevarious CoA concentrations (2.5 -30 μM) and the fixed apo-ACPconcentrations (0.25 (),0.35 (▪), 0.5 (▴), and 0.6 μM (♦)). B:double-reciprocal plots of the initial velocities of AcpS versus thevarious apo-ACP concentrations (0.25-0.6 μM) and the fixed CoAconcentrations (2.5 () , 5.0 (▪), 10 (▴), and 20 μM (♦)).

[0046]FIG. 7 shows an analysis of the inhibition kinetics of 3′,5′-ADPwith respect to apo-ACP and CoA. AcpS activity is measured in theabsence () or presence of 3′,5′-ADP (5 (▪) and 10 μM (▴)). A and B: thedouble-reciprocal plots of the initial 2 5 velocities of AcpS versus thevarious CoA concentrations and the fixed apo-ACP concentration, and thevarious apo-ACP concentrations and the fixed CoA concentrations,respectively. C and D: Dixon plots of A and B, respectively. The CoAconcentrations used in panel C are 10 () and 40 (▪) μM.

[0047]FIG. 8A is a color stereoview showing a ribbon diagram of the AcpShomotrimer, viewed along a non-crystallographic 3-fold axis.

[0048]FIG. 8B is a color ribbon diagram of the Cα backbone of oneStreptococcus pneumoniae AcpS monomer structure.

[0049]FIG. 8C is a color topology (Richardson) diagram of AcpS.β-strands are represented as arrows, while α helices are rectangles. Thesecondary structure elements are defined as follows: β1, Ile4-Glu13; α1,Leu14-Arg23; α2, Phe27-Val31; α3, Ala34-Ser42; α4, Gly45-Met66; α5,Ile70-Leu73; β2, Glu79-Asn82; β3, Pro88-Gln92; β4, Lys98-His105; β5,Phe109-Glu117.

[0050]FIG. 9 is a color stereoview of the 3′,5′-ADP fragment of CoAbound to the active site of S. pneumoniae AcpS. The omitted electrondensity map corresponding to the ligand is contoured at the 1 σ level at1.9 Å resolution.

[0051]FIG. 10 shows a color superposition of apo-AcpS from S. pneumoniae(shown in blue) on the surfactin synthetase activating enzyme Sfp(4′-phosphopantetheinyl transferase) from Bacillus subtilis complexedwith CoA (shown in red). One protomer of AcpS is superimposed on theN-terminal domain of Sfp, and a second AcpS protomer is superimposed onthe C-terminal domain of Sfp. The third protomer of the AcpS trimer doesnot have a counterpart in the Sfp structure. A sulfate ion is found inthe AcpS binding site that corresponds to the position of theα-phosphate of CoA in the Sfp molecule.

[0052] Table 1A shows sequence alignment of bacterial AcpS genes fromdifferent species. The most conserved regions are shown in grey.Secondary structural elements observed in the S. pneumoniae AcpS crystalstructure are indicated above the sequence pile-up.

[0053] Table 1B shows structural alignment of two Streptococcuspneumoniae AcpS monomer molecules with two domains of Bacillus subtilisSfp. The N-terminal half of Sfp from Metl to ProlO3 corresponds to oneprotomer of the AcpS trimer (shown in blue), and has a 22% sequenceidentity. The C-terminal half of Sfp from Ile104 to Pro209 correspondsto a second AcpS protomer (shown in green) and has 25% sequenceidentity. The remaining C-terminal portion from Asp210 to Leu224 has nocounterpart in the AcpS structure. The three amino acid residuesinvolved in Mg²⁺ binding are marked by an asterisk (*). The regionsinvolved in CoA binding are marked by plus (+) signs.

[0054] Table 2 (1 page) summarizes the crystallographic data disclosedherein.

[0055] Table 3 (51 pages) shows the atomic coordinates for AcpS native1.

[0056] Table 4 (52 pages) shows the atomic coordinates for AcpS native2.

[0057] Table 5 (53 pages) shows the atomic coordinates forAcpS/3′,5′-ADP complex.

[0058] The tables herein are presented after the Abstract of theDisclosure.

DETAILED DESCRIPTION OF THE INVENTION

[0059] The following detailed description of the invention is providedto aid those skilled in the in art in practicing the present invention.Even so, the following detailed description should not be construed tounduly limit the present invention as modifications and variations inthe embodiments discussed herein can be made by those of ordinary skillin the art without departing from the spirit or scope of the presentinventive discovery.

[0060] The contents of each of the references cited herein are hereinincorporated by reference in their entirety.

[0061] The present invention provides novel Streptococcus pneumoniaeAcpS crystal structures, including their active sites, use of thesecrystal structures to produce antibodies to epitopes of this protein forin vitro and in vivo diagnostic purposes, and methods of using thesecrystal structures and active sites to identify or design AcpS inhibitorcompounds for use as antibacterials in the treatment of bacterialinfections. Among its many aspects, the present invention provides amethod for inhibiting AcpS by administering compounds having certainstructural, physical, and spatial characteristics that permitinteraction, e.g., binding, of such compounds with specific amino acidresidues within acyl carrier protein synthases, particularly the activesites of these enzymes. Such compounds may bind to all or only a portionof an active site, and may be competitive or non-competitive inhibitorsof these enzymes.

[0062] As used herein, the term “crystal” includes an ordered proteinarray having a regular structure of a constituent chemical species,e.g., such as an AcpS protein or portion thereof. In one embodiment, acrystal of the present invention comprises a solid three-dimensionalAcpS protein aggregate in which planar surfaces intersect at definiteangles. In another embodiment, a crystal of the invention comprises anordered two dimensional packing of AcpS proteins, such as, e.g., in amonolayer.

[0063] As used herein, the term “active site” refers to the generalregion of an enzyme molecule containing the catalytic residuesidentified with the binding of substrate(s) (and prosthetic group(s), ifany), and reaction of substrate(s) by the making and breaking of bonds.“Catalytic residues” include any of the amino acid residues in an enzymethat are directly involved in making or breaking covalent bonds whilethe enzyme is acting on a substrate. It includes those amino acidresidues that are, in the enzyme-substrate complex, either contact aminoacids, i.e., those that at some point are within only one bond distanceof some point on the substrate molecule (which may include bothcatalytic residues and specificity residues), or auxiliary amino acids,i.e., those that are not in such intimate physical contact with thesubstrate, but which nonetheless play a definite role in the action ofthe enzyme. The active site generally takes up a relatively small partof the total volume of an enzyme molecule. Most of the amino acidsresidues in an enzyme are not in contact with the substrate. The activesite is a three-dimensional entity, often a cleft or crevice, formed bygroups that come from different parts of the linear amino acid sequence.Residues far apart in the linear sequence may interact more stronglythan adjacent residues in the amino acid sequence. Substrates are boundto enzymes by multiple weak attractions, including electrostatic bonds,hydrogen bonds, van der Waals forces, and hydrophobic interactions. Theenzyme and substrate should have complementary shapes. Finally, thespecificity of binding depends on the precisely defined arrangement ofatoms in the active site, and the shapes of the active sites of someenzymes are markedly modified by the binding of substrate. Thus, theactive sites of these enzymes have shapes that are complementary to thatof the substrate only after the substrate is bound, a process of dynamicrecognition called “induced fit.”

[0064] Inhibitors of acyl carrier protein synthases are predicted tointeract with (bind) these proteins in the region comprising the3′,5′-adenosine diphosphate binding site, shown in FIG. 9.

[0065] As used herein, including the appended claims, singular forms ofwords such as “a,” “an,” and “the” include, e.g., their correspondingplural referents unless the context clearly dictates otherwise. Thus,for example, reference to “a crystal” includes, e.g., one or morecrystals, reference to “an AcpS crystal” includes, e.g., one or more ofsuch crystals; reference to a binding event includes one or more suchevents; reference to bind a crystal includes binding one or more suchcrystals; and reference to “a method” includes, e.g., reference toequivalent steps and methods known to a person of ordinary skill in theart, and so forth.

[0066] With respect to antibodies for diagnostic purposes, the crystalstructures disclosed herein facilitate the production of suchantibodies. Knowledge of the three-dimensional structure of AcpSprovides information as to various epitopes on the enzyme surface. Usingthis knowledge, one can synthesize peptides comprising such epitopes,and produce antibodies that specifically bind thereto by methods wellknown in the art. Antibodies produced in response to these peptides canthen be used to detect the presence of Streptococcus pneumoniae both invitro and in vivo, thereby providing useful diagnostic means fordetecting the presence of this pathogen.

[0067] Structure-Based Drug Design

[0068] The use of protein crystal structures to design candidateantimicrobial compounds can be accomplished by structure-based drugdesign. In one embodiment of this method, the three-dimensionalstructure of a protein or protein fragment, such as a peptide, isdetermined, and potential antagonists (or agonists, if desired) aredesigned with the aid of computer modeling (Bugg et al.,1993; West etal., 1995). Once the crystal structure of the target, e.g.,Streptococcus pneumoniae AcpS is determined, computer modeling isconducted (using programs such as DOCK or Multiple Copy SimultaneousSearch (MCSS)) to construct candidate inhibitor compounds based on thecrystal structure. These compounds are chemically synthesized, orobtained from previously existing drug libraries, and their binding tothe AcpS target and/or their biological activity, i.e., inhibitoryactivity, against AcpS is assayed. Compounds that bind and/or thatinhibit the enzymatic activity of AcpS are thereby identified as drugcandidates. In a further refinement of this method, those compoundsexhibiting binding and/or activity can be associated or complexed withthe crystal for further X-ray diffraction analysis to map theirinteractions with the crystal structure. This can be accomplished bygrowing a supplemental crystal of AcpS in the presence of one suchcompound to produce a crystal containing a complex formed between theAcpS protein and the drug candidate. A crystal is chosen thateffectively diffracts X-rays, allowing the determination of the atomiccoordinates of the protein-ligand complex to a resolution greater thanabout 10 Å, preferably to a resolution greater than about 5 Å, morepreferably to a resolution greater than about 3 Å, more preferably to aresolution greater than about 2.0 Å, and most preferably to a resolutionof about 1.9 Å. The three-dimensional structure of the supplementalcrystal is determined by molecular replacement analysis, and a drug isselected by performing rational drug design with the three-dimensionalstructure determined using the supplemental crystal. Such selecting ispreferably performed in conjunction with computer modeling.

[0069] From the resulting inhibitor-target crystal structure, one ofordinary skill in the art can construct further improved candidatecompounds.

[0070] The steps set forth in the preceding paragraphs can be repeatedand refined as desired until a drug candidate having the desired potencyis identified.

[0071] Protein Expression

[0072] As would be apparent to those of ordinary skill in the art,conventional molecular biological, microbiological, and recombinant DNAtechniques are available that permit expression of amounts of AcpSprotein sufficient for the types of studies described herein usinggenomic DNA, cDNA, synthetic DNA, etc. coding on expression therefor.Such techniques are fully explained in the literature, e.g., Sambrook etal., 1989 and Ausubel et al., 1987. Note also in this regard U.S. Pat.Nos. 6,020,162 and 6,087,478.

[0073] Preparation of Protein Crystals

[0074] Crystals of AcpS can be grown by a number of techniques,including batch crystallization, vapor diffusion (either by sittingdrop, hanging drop, or sandwich), microdialysis, membranecrystallization, or any other conventional method of proteincrystallization. Seeding of crystals is sometimes required in order toobtain X-ray quality crystals. Standard micro- and/or macro-seeding ofcrystals can therefore be employed. As described below, the hanging dropmethod can be used to obtain the crystals disclosed herein.

[0075] X-ray Diffraction

[0076] Once a crystal of the present invention is grown, X-raydiffraction data can be collected. Crystals can be characterized, forexample, by using X-rays produced in a conventional source (such as asealed tube or a rotating anode), or using a synchrotron source. Methodsof characterization include, but are not limited to, precisionphotography, oscillation photography, and diffractometer datacollection. Heavy atom derivatives, such as produced using Hg, Pb, Au,U, Pt, I, Os, etc., can be performed using Fuji imaging plates.Alternatively, AcpS can be synthesized with selenium-methionine (Se-Met)in place of methionine, and the Se-Met multiwavelength anomalousdispersion data (Hendrickson, 1991) can be collected on CHESS F2, usingreverse-beam geometry to record Friedel pairs at four X-ray wavelengths,corresponding to two remote points above and below the Se absorptionedge (λ₁ and λ₄) and the absorption edge inflection point (λ₂) and peak(λ₃). Selenium sites can be located using SHELXS-90 in Patterson searchmode (G. M. Sheldrick). Experimental phases (α_(MAD)) can be estimatedvia a multiple isomorphous replacement/anomalous scattering strategyusing MLPHARE (Z. Otwinowski, Southwestern University of Texas, Dallas)with three of the wavelengths treated as derivatives and one (λ₂)treated as the parent for example. In either case, data can be processedusing HKL, DENZO, and SCALEPACK (Otwinowski and Minor, 1997).

[0077] In addition, X-PLOR (Brünger, 1992; X-PLOR v. 3.1 Manual, NewHaven, Yale University) or Heavy (T. Terwilliger, Los Alamos NationalLaboratory) can be utilized for bulk solvent correction and B-factorscaling. After density modification and non-crystallographic averaging,the protein is built into an electron density map using the program O(Jones et al., 1991). Model building interspersed with positional andsimulated annealing refinement (Brünger, 1992, supra) can permit theunambiguous trace and sequence assignment of the AcpS protein.

[0078] Protein-Structure Based Design of Agonists and Antagonists ofAcpS

[0079] Once the three-dimensional structure of a crystal comprising theAcpS protein, or fragment or fusion protein derivative thereofcomprising an active site, is determined, a potential ligand (antagonistor agonist) can be examined via the use of computer modeling using adocking program such as RAM, DOCK, or AUTODOCK (Dunbrack et al., 1997).This procedure can include computer fitting of potential ligands to AcpSto ascertain how well the shape and the chemical structure of thepotential ligand will complement or interfere with the enzyme (Bugg etal., 1993; West et al., 1995). Computer programs can also be employed toestimate the attraction, repulsion, and steric hindrance of the ligandto the AcpS binding site. Generally the tighter the fit (e.g., the lowerthe steric hindrance, and/or the greater the attractive force) the morepotent the potential drug will be since these properties are consistentwith a tighter binding constant. Furthermore, the greater thespecificity in the design of a potential drug, the more likely that thedrug will not interfere with other properties of the AcpS protein orother proteins in host cells. This will minimize potential side-effectsdue to unwanted interactions with other proteins.

[0080] Initially, a potential ligand could be obtained by screening, forexample, a random peptide library produced by recombinant bacteriophage(Scott et al., 1990; Cwirla et al., 1990; Devlin et al., 1990) or achemical library. A ligand selected in this manner could be then besystematically modified by computer modeling programs until one or morepromising potential ligands are identified. Such analysis has been shownto be effective in the development of HIV protease inhibitors (Lam etal., 1994; Wlodawer et al., 1993; Appelt, 1993; Erickson, 1993).

[0081] Such computer modeling allows the selection of a finite number ofrational chemical modifications, as opposed to the countless number ofessentially random chemical modifications that could be made, and ofwhich any one might lead to a useful drug. Each chemical modificationrequires additional chemical steps, which while being reasonable for thesynthesis of a finite number of compounds, quickly becomes overwhelmingif all possible modifications needed to be synthesized. Thus, throughthe use of the three-dimensional structure disclosed herein incombination with computer modeling, a large number of these compoundscan be rapidly screened on the computer monitor screen, and a few likelycandidates can be determined without the laborious synthesis of untoldnumbers of compounds.

[0082] Once a potential ligand (agonist or antagonist) is identified, itcan either be selected from a library of chemicals as are commerciallyavailable from most large chemical companies including Eli Lilly andCompany, or alternatively, the potential ligand can be synthesized denovo. As noted above, the de novo synthesis of one or even a relativelysmall group of specific compounds is reasonable in the art of drugdesign. The prospective drug can be placed into any standard bindingassay described below to test its effect on the AcpS protein.

[0083] When a suitable drug is identified, a supplemental crystal can begrown which comprises a protein-ligand complex formed between the AcpSprotein and the drug.

[0084] Preferably, the crystal effectively diffracts X-rays, allowingthe determination of the atomic coordinates of the protein-ligandcomplex to a resolution of greater than about 5.0 Å, more preferablygreater than about 3.0 Å, and even more preferably greater than about2.0 Å. The three-dimensional structure of the supplemental crystal canbe determined by molecular replacement analysis. Molecular replacementinvolves using a known three-dimensional structure as a search model todetermine the structure of a closely related molecule or protein-ligandcomplex in a new crystal form. The measured X-ray diffraction propertiesof the new crystal are compared with the search model structure tocompute the position and orientation of the protein in the new crystal.Computer programs that can be used for this purpose include X-PLOR andAMORE (J. Navaza, 1994). Once the position and orientation are known, anelectron density map can be calculated using the search model to provideX-ray phases. Thereafter, the electron density is inspected forstructural differences, and the search model is modified to conform tothe new structure. Using this approach, it will be possible to use theclaimed structure of the AcpS protein to solve the three-dimensionalstructures of any such AcpS protein. Other computer programs that can beused to solve the structures of such AcpS crystals include QUANTA,CHARMM. INSIGHT, SYBYL, MACROMODE, and ICM.

[0085] For all of the drug screening assays described herein, furtherrefinements to the structure of the drug will generally be necessary andcan be made by the successive iterations of any and/or all of the stepsprovided by the particular drug screening assay.

[0086] Binding and Other Assays for Drug Screening

[0087] Once identified by computer modeling techniques, candidatecompounds can be tested for biological activity using standardtechniques. For example, such compounds can be used in assays to assessinhibition of AcpS enzymatic activity, or binding assays usingconventional formats to screen inhibitors. Examples of such assaysinclude enzyme-linked immunosorbent assays (ELISA) or fluorescencequench assays. Such compounds can also be tested in in vitro assaysdesigned to assess growth inhibition or killing of the microorganismharboring such enzymes, or in vivo in infected hosts.

[0088] It should be noted that the present invention encompasses the useof analogs and derivatives that have the same or substantially similarenzymatic activity as that of the Streptococcus pneumoniae AcpS proteinexemplified herein. Such derivatives and analogs include, but are notlimited to, AcpS proteins containing amino acid additions,substitutions, or deletions that result in proteins functionallyequivalent to the Streptococcus pneumoniae AcpS protein disclosedherein.

[0089] AcpS Peptide, Polvpeptide, and Protein Variants

[0090] The present invention encompasses AcpS having the amino acidsequence shown in SEQ ID NO: 1, as well as fragments of this proteincontaining an active site, fusions of AcpS with other proteins, fusionsof fragments of this protein containing an active site, as well as aminoacid variants of any of these sequences that retain AcpS enzymaticactivity.

[0091] The peptides, polypeptides, and proteins of the presentinvention, or variants thereof, can comprise any number of contiguousamino acid residues. The subsequence of contiguous amino acids derivedfrom the protein sequence disclosed herein can be at least about 20, atleast about 30, at least about 40, at least about 50, at least about 60,at least about 70, at least about 80, or at least about 90 amino acidsin length. Furthermore, the number of contiguous amino acid residues insuch subsequences can be any integer selected from the group consistingof from 1 to 20, such as 2, 3, 4, or 5.

[0092] In a further aspect, the present invention encompasses anisolated AcpS peptide, polypeptide, or protein comprising an amino acidsequence having at least about 80% sequence identity, preferably atleast about 81% sequence identity, more preferably at least about 82%sequence identity, yet more preferably at least about 83% sequenceidentity, yet more preferably at least about 84% sequence identity, yetmore preferably at least about 85% sequence identity, yet morepreferably at least about 86% sequence identity, yet more preferably atleast about 87% sequence identity, yet more preferably at least about88% sequence identity, yet more preferably at least about 89% sequenceidentity, yet more preferably at least about 90% sequence identity, yetmore preferably at least about 91% sequence identity, yet morepreferably at least about 92% sequence identity, yet more preferably atleast about 93% sequence identity, yet more preferably at least about94% sequence identity, yet more preferably at least about 95% sequenceidentity, yet more preferably at least about 96% sequence identity, yetmore preferably at least about 97% sequence identity, yet morepreferably at least about 98% sequence identity, and even yet morepreferably at least about 99% sequence identity, to the correspondingregion of the AcpS protein of the present invention (SEQ ID NO: 1).

[0093] In a further aspect, the present invention relates to an isolatedpeptide, polypeptide, or protein comprising an amino acid sequencescoring at least about 80% positives, preferably at least about 81%positives, more preferably at least about 82% positives, yet morepreferably at least about 83% positive, yet more preferably at leastabout 84% positives, yet more preferably at least about 85% positives,yet more preferably at least about 86% positives, yet more preferably atleast about 87% positives, yet more preferably at least about 88%positives, yet morepreferably at least about 89% positives, yet morepreferably at least about 90% positives, yet more preferably at leastabout 91% positives, yet more preferably at least about 92% positives,yet more preferably at least about 93% positives, yet more preferably atleast about 94% positives, yet more preferably at least about 95%positives, yet more preferably at least about 96% positives, yet morepreferably at least about 97% positives, yet more preferably at leastabout 98% positives, yet more preferably at least about 99% positives,when compared with the amino acid sequence of corresponding residuesshown in SEQ ID NO:1.

[0094] The present invention encompasses biochemically active variantsof the AcpS protein disclosed herein. Biochemical activity includes, forexample, AcpS enzymatic activity. Such biochemically active peptides,polypeptides, and proteins have activity that is at least about 20%,30%, or 40%, preferably at least about 50%, 60%, or 70%, and mostpreferably at least about 80%, 90%, or 95%-100% of that of thecorresponding native (non-synthetic) AcpS protein. Furthermore, theligand binding specificity of such variant AcpS molecules issubstantially similar to that of the corresponding native(non-synthetic) protein. Typically, the ligand binding specificity willbe at least about 30%, 40%, or 50% that of the corresponding native(non-synthetic) protein, and more preferably at least about 60%, 70%,80%, or 90%-100% thereof. Methods of assaying and quantifying measuresof biochemical activity and ligand binding by AcpS are described herein;others are well known to those of skill in the art.

[0095] The term “amino acid” is used herein in its broadest sense, andincludes naturally occurring amino acids as well as non-naturallyoccurring amino acids, including amino acid analogs and derivatives. Thelatter includes molecules containing an amino acid moiety. One skilledin the art will recognize, in view of this broad definition, thatreference herein to an amino acid includes, for example, naturallyoccurring proteogenic L-amino acids; D-amino acids; chemically modifiedamino acids such as amino acid analogs and derivatives; naturallyoccurring non-proteogenic amino acids such as norleucine, β-alanine,ornithine, etc.; and chemically synthesized compounds having propertiesknown in the art to be characteristic of amino acids. As used herein,the term “proteogenic” indicates that the amino acid can be incorporatedinto a peptide, polypeptide, or protein in a cell through a metabolicpathway.

[0096] In addition to using D-amino acids, those of ordinary skill inthe art are aware that modifications in the amino acid sequence of apeptide, polypeptide, or protein can result in equivalent, or possiblyimproved, second generation peptides, etc., that display equivalent orsuperior functional characteristics when compared to the original aminoacid sequences. Alterations in the AcpS peptides, polypeptides, orproteins of the present invention can include one or more amino acidinsertions, deletions, substitutions, truncations, fusions, shuffling ofsubunit sequences, and the like, either from natural mutations or humanmanipulation, provided that the sequences produced by such modificationshave substantially the same (or improved or reduced, as may bedesirable) activity(ies) as the naturally occurring counterpartsequences disclosed herein.

[0097] One factor that can be considered in making such changes is thehydropathic index of amino acids. The importance of the hydropathicamino acid index in conferring interactive biological function on aprotein has been discussed by Kyte and Doolittle (1982). It is acceptedthat the relative hydropathic character of amino acids contributes tothe secondary structure of the resultant protein. This, in turn, affectsthe interaction of the protein with molecules such as enzymes,substrates, receptors, ligands, DNA, antibodies, antigens, etc. Based onits hydrophobicity and charge characteristics, each amino acid has beenassigned a hydropathic index as follows: isoleucine (+4.5); valine(+4.2); leucine (+3.8); phenylalanine (+2.8); cysteine/cystine (+2.5);methionine (+1.9); alanine (+1.8); glycine (−0.4); threonine (−0.7);serine (−0.8); tryptophan (−0.9); tyrosine (−1.3); proline (−1.6);histidine (−3.2); glutamate/glutamine/aspartate/asparagine (−3.5);lysine (−3.9); and arginine (−4.5).

[0098] As is known in the art, certain amino acids in a peptide,polypeptide, or protein can be substituted for other amino acids havinga similar hydropathic index or score and produce a resultant peptide,etc., having similar biological activity, i.e., which still retainsbiological functionality. In making such changes, it is preferable thatamino acids having hydropathic indices within ±2 are substituted for oneanother. More preferred substitutions are those wherein the no acidshave hydropathic indices within ±1. Most preferred substitutions arethose wherein the amino acids have hydropathic indices within ±0.5.

[0099] Like amino acids can also be substituted on the basis ofhydrophilicity. U.S. Pat. No. 4,554,101 discloses that the greatestlocal average hydrophilicity of a protein, as governed by thehydrophilicity of its adjacent amino acids, correlates with a biologicalproperty of the protein. The following hydrophilicity values have beenassigned to amino acids: arginine/lysine (+3.0); aspartate/glutamate(+3.0±1); serine (+0.3); asparagine/glutamine (+0.2); glycine (0);threonine (−0.4); proline (−0.5±1); alanine/histidine (−0.5); cysteine(−1.0); methionine (−1.3); valine (−1.5); leucine/isoleucine (−1.8);tyrosine (−2.3); phenylalanine (−2.5); and tryptophan (−3.4). Thus, oneamino acid in a peptide, polypeptide, or protein can be substituted byanother amino acid having a similar hydrophilicity score and stillproduce a resultant peptide, etc., having similar biological activity,i.e., still retaining correct biological function. In making suchchanges, amino acids having hydropathic indices within ±2 are preferablysubstituted for one another, those within ±1 are more preferred, andthose within ±0.5 are most preferred.

[0100] As outlined above, amino acid substitutions in the AcpS moleculesof the present invention can be based on the relative similarity of theamino acid side-chain substituents, for example, their hydrophobicity,hydrophilicity, charge, size, etc. Exemplary substitutions that takevarious of the foregoing characteristics into consideration in order toproduce conservative amino acid changes resulting in silent changeswithin the present peptides, etc., can be selected from other members ofthe class to which the naturally occurring amino acid belongs. Aminoacids can be divided into the following four groups: (1) acidic aminoacids; (2) basic amino acids; (3) neutral polar amino acids; and (4)neutral non-polar amino acids. Representative amino acids within thesevarious groups include, but are not limited to: (1) acidic (negativelycharged) amino acids such as aspartic acid and glutamic acid; (2) basic(positively charged) amino acids such as arginine, histidine, andlysine; (3) neutral polar amino acids such as glycine, serine,threonine, cysteine, cystine, tyrosine, asparagine, and glutamine; and(4) neutral non-polar amino acids such as alanine, leucine, isoleucine,valine, proline, phenylalanine, tryptophan, and methionine.

[0101] Particularly preferred conserved amino acid substitutions are:

[0102] (a) Lys for His or for Arg, or vice versa, such that a positivecharge is maintained;

[0103] (b) Glu for Asp, or vice versa, such that a negative charge ismaintained;

[0104] (c) Ser for Thr, or vice versa, such that a free —OH group ismaintained;

[0105] (d) Gln for Asn, or vice versa, such that a free —NH₂ group ismaintained;

[0106] (e) Ile for Leu or for Val, or vice versa, as roughly equivalenthydrophobic amino acids; and

[0107] (f) Phe for Tyr, or vice versa, as roughly equivalent aromaticamino acids.

[0108] Non-conservative amino acid substitutions can also be introducedif they do not substantially affect either the ligand binding orenzymatic properties of the AcpS protein. Such non-conservative aminoacid substitutions can occur in regions of the protein not involved indrug candidate binding, but can also be tolerated in regions involved insuch binding if they do not significantly affect such binding, i.e.,binding of the ligand occurs substantially the same as in the wild-typeStreptococcus pneumoniae AcpS protein. It should be noted that changesthat are not expected to be advantageous can also be useful if theseresult in the production of functional sequences. Since small peptides,etc., can be easily produced by conventional solid phase synthetictechniques, the present invention includes peptides, etc., such as thosediscussed herein, containing the amino acid modifications discussedabove, alone or in various combinations. To the extent that suchmodifications can be made while substantially retaining the activity ofthe peptide, etc., they are included within the scope of the presentinvention. The utility of such modified peptides, etc., can bedetermined without undue experimentation by, for example, the methodsdescribed herein.

[0109] While biologically functional equivalents of the present AcpSmolecules can have any number of conservative or non-conservative aminoacid changes that do not significantly affect their activity(ies), orthat increase or decrease activity as desired, 40, 30, 20, 10, 5, or 3changes, such as 1-30 changes or any range or individual value therein,may be preferred. In particular, 10 or fewer amino acid changes may bepreferred. More preferably, seven or fewer amino acid changes may bepreferred; more preferably, five or fewer amino acid changes may bepreferred; most preferably, three or fewer amino acid changes may bepreferred. The encoding nucleotide sequences (gene, plasmid DNA, cDNA,synthetic DNA, or mRNA, for example) will thus have corresponding basesubstitutions, permitting them to code on expression for thebiologically functional equivalent forms of the AcpS molecules. In anycase, the AcpS peptides, polypeptides, or proteins exhibit the same orsimilar biological or immunological activity(ies) as that(those) of theAcpS molecule specifically dislcosed herein, or increased or reducedactivity, if desired.

[0110] The activity(ies) of the variant AcpS molecules can be determinedby the methods described herein or as are known in the art. Variant AcpSmolecules biologically functionally equivalent to those specificallydisclosed herein have activity(ies) differing from those of thepresently disclosed molecules by about ±50% or less, preferably by about±40% or less, more preferably by about ±30% or less, more preferably byabout ±20% or less, more preferably by about ±10% or less, and even morepreferably by about ±5% or less, when assayed by the methods disclosedherein, or as are known in the art.

[0111] Amino acids in an AcpS molecule of the present invention that areessential for activity can be identified by methods known in the art,such as site-directed mutagenesis or alanine-scanning mutagenesis(Cunningham and Wells, 1989). The latter procedure introduces singlealanine mutations at every residue in the molecule. The resulting mutantmolecules are then tested for biological activity. Sites that arecritical for ligand binding can also be identified by structuralanalysis such as crystallization, nuclear magnetic resonance, orphotoaffinity labeling (Smith et al., 1992, and de Vos et al., 1992).

[0112] Methods of Drug Discovery/Design Using the Three-DimensionalStructure of Crystallized AcpS

[0113] The three-dimensional crystal structures and atomic coordinatesdisclosed herein can be used to model an AcpS. These atomic coordinatescan be used to computationally design a chemical compound that binds tothe active site of an AcpS, and inhibit the enzymatic activity thereof.Such chemical compounds can be used to treat or prevent a Streptococcuspneumoniae infection in a mammal in need thereof.

[0114] Numerous methods can be employed to discover/design compoundsthat bind to AcpS, inhibit its activity, and that can therefore exhibiteffective antibacterial activity. It should be noted that in all themethods described herein, one can employ the atomic coordinates of theentire AcpS protein, or just those of an active site.

[0115] For example, one method of drug design comprises employing thestructural coordinates of a crystal of Streptococcus pneumoniae AcpS tocomputationally evaluate the ability of a chemical compound to interactwith, e.g., bind to an active site of, the AcpS. Such chemical compoundcan be a competitive, non-competitive, uncompetitive, or mixed inhibitorthat binds to, or inhibits the enzymatic activity of, AcpS. For example,the compound can be a competitive inhibitor that binds to the catalyticactive site of AcpS.

[0116] Another method comprises employing the structural coordinates ofa crystal of Streptococcus pneumoniae AcpS to identify an intermediatein a biochemical reaction between AcpS and a compound that is asubstrate or inhibitor of this enzyme.

[0117] Another method of designing a candidate compound that binds to orinhibits Streptococcus pneumoniae AcpS comprises:

[0118] (a) providing the three-dimensional structure of a crystal ofStreptococcus pneumoniae AcpS defined by the atomic coordinates shown inTables 3 and 4, wherein the atomic coordinates include the active siteof the synthase; and

[0119] (b) designing a candidate compound based upon thethree-dimensional crystal structure of the active site of the enzyme.

[0120] Another method of designing a compound useful for inhibitingStreptococcus pneumoniae AcpS comprises:

[0121] (a) obtaining a crystal of Streptococcus penumoniae AcpS;

[0122] (b) evaluating the three-dimensional structure of the crystal;

[0123] (c) synthesizing or obtaining from a pre-existing chemical orcomputer library a potential inhibitor compound based on thethree-dimensional crystal structure of the crystal;

[0124] (d) contacting the Streptococcus pneumoniae AcpS and thepotential inhibitor compound; and

[0125] e) assaying the Streptococcus pneumoniae AcpS for activity,wherein a decrease in activity of the AcpS in the presence of thecompound compared to the activity of the AcpS in the absence of thecompound identifies the compound as an inhibitor of Streptococcuspneumoniae AcpS.

[0126] Another method of identifying a compound that binds to andinhibits the enzymatic activity of Streptococcus pneumoniae AcpS or anyother AcpS comprising the same or similar active site coordinates(active site configuration) as those of Streptococcus pneumoniae AcpScomprises:

[0127] (a) introducing into a suitable computer program, e.g., a dockingprogram, an algorithm for structure-based ligand design/optimization,etc., information defining the conformation of the catalytic active siteof Streptococcus pneumoniae AcpS, wherein the program displays thethree-dimensional structure of the catalytic active site;

[0128] (b) creating a three-dimensional representation of the activesite cavity of the Streptococcus pneumoniae AcpS in the computerprogram;

[0129] (c) displaying and superimposing a model of the compound on thethree-dimensional representation of the active site cavity of the AcpS;

[0130] (d) assessing whether the compound model fits spatially into theactive site;

[0131] (e) incorporating the compound in a biological or biochemicalactivity assay for an AcpS comprising the active site; and

[0132] (f) determining whether the compound inhibits AcpS activity inthe assay.

[0133] In another method, the coordinates in Tables 3 and 4 can be usedto identify the active site of AcpS, and the obtained information canthen be used for visual analysis/inspection of enzyme/inhibitorinteractions to identify a compound that inhibits the function of AcpS.

[0134] Another method of identifying an inhibitor of AcpS activitycomprises docking a computer representation of a first compoundstructure with a computer representation of the structure of the cavityformed by the active site of an AcpS, thereby forming a complex betweenthe first compound and the AcpS. The method can further comprise:

[0135] (a) removing the computer representation of the first compoundfrom the active site, and docking a computer representation of a secondcompound selected from a computer data base with the computerrepresentation of the active site, thereby forming a second complexcomprising the second compound and the AcpS active site;

[0136] (b) determining a conformation of the second complex of step (a)with a favorable geometric fit and favorable complementary interactions;and

[0137] (c) identifying a compound that best fits the active site as apotential modulator of the AcpS activity.

[0138] This method can further comprise:

[0139] (a) modifying the computer representation of the first compoundby deleting one or more chemical groups from the first compound, or byadding one or more chemical groups to the first compound, therebyforming a second complex;

[0140] (b) determining a conformation of the second complex of step (a)with a favorable geometric fit and favorable complementary interactions;and

[0141] (c) identifying a compound that best fits said active site as apotential modulator of the AcpS activity.

[0142] This method can further comprise:

[0143] (a) removing the computer representation of the first compoundcomplexed with the AcpS active site; and

[0144] (b) searching a database for a second compound structurallysimilar to the first compound using a compound searching computerprogram, or replacing portions of the first compound with chemicalstructures from a database using a compound construction computerprogram.

[0145] Furthermore, structural information on the interaction of acompound with AcpS can be used to place another compound in the activesite, or to perform a virtual screen of a computer library of compoundsto identify a lead compound by structure-based drug design.

[0146] The foregoing methods can further comprise:

[0147] (a) incorporating the second compound in a biological orbiochemical activity assay for an AcpS comprising the active site; and

[0148] (b) determining whether the second compound inhibits the AcpSenzymatic activity in the assay.

[0149] Another method of identifying an inhibitor that competitivelybinds to the active site of Streptococcus pneumoniae AcpS or other acylcarrier protein synthase having the same or similar active site atomiccoordinates comprises:

[0150] (a) providing the atomic coordinates of the active site to acomputerized modeling system;

[0151] (b) identifying a compound that binds to the active site; and

[0152] (c) screening the compound identified in step (b) for AcpSinhibitory activity.

[0153] Another method of the present invention encompasses solving acrystal structure by using the structural coordinates of Streptococcuspneumoniae AcpS, or a portion thereof, as disclosed herein to solve acrystal form of a mutant, homologue, or co-complex of this AcpS bymolecular rearrangement.

[0154] Yet other methods of the present invention relate to determiningthe three-dimensional structure of AcpS enzymes of unknown structure byusing information derived from the three-dimensional structure of AcpSas disclosed herein. One such method comprises:

[0155] (a) aligning a computer representation of the amino acid sequenceof Streptococcus pneumoniae AcpS with a computer representation of theamino acid sequence of another acyl carrier protein synthase by matchinghomologous regions of amino acid sequences of these representations;

[0156] (b) transferring computer representations of the amino acidsequence in said other acyl carrier protein synthase to computerrepresentations of corresponding amino acid sequences in thethree-dimensional structure of Streptococcus pneumoniae AcpS; and

[0157] (c) determining a low energy conformation of the other acylcarrier protein synthase structure resulting from step (b).

[0158] Another such method of determining the three-dimensionalstructure of an acyl carrier protein synthase of unknown structurecomprises:

[0159] (a) determining the secondary structure of Streptococcuspneumoniae AcpS having the structural atomic coordinates set forth inTables 3 and 4 using NMR data; and

[0160] (b) simplifying the assignment of through-space interactions ofamino acids.

[0161] Another method encompassed by the present invention is one fordesigning a ligand that binds to the active site domain of AcpS. Suchmethod can be computer-based, and can comprise:

[0162] (a) providing a model of the crystal structure of the active sitedomain of Streptococcus pneumoniae AcpS;

[0163] (b) analyzing the model to design a ligand that binds to theactive site domain; and

[0164] (c) determining the effect of the ligand on the active site.

[0165] Such an effect might be a conformational change in the activesite, covalent bond formation, etc. This method can further comprisemodifying the ligand to improve the binding affinity to AcpS,selectivity to AcpS, or both, of the ligand.

[0166] Also encompassed by the present invention are antibacterialcompounds that modulate AcpS activity, by, for example, binding toand/or inhibiting AcpS, discovered or designed by any of the foregoingmethods. Non-limiting examples of such compounds include a compoundselected from a computer database, a compound constructed from chemicalgroups selected from a computer database, a chemically synthesizedcompound, a naturally occurring compound, a peptide, peptidomimetic, ora natural product molecule that binds in the active site ofStreptococcus pneumoniae AcpS.

[0167] Such compounds can be used in methods of preventing or treating aStreptococcus pneumoniae infection, or other infection caused by amicroorganism having an AcpS enzyme, by administering to a patient inneed thereof a pharmaceutically effective amount of such compound.

[0168] In addition to the foregoing applications of AcpS crystals, thepresent invention also encompasses the use of such crystals for avariety of other purposes, such as those discussed below.

[0169] AcpS Crystalline Compositions

[0170] Enzymes can be employed in a variety functions, such as, forexample, as catalysts in large and/or laboratory scale economicalproduction of fine and specialty chemicals (Jones, J. B., Tetrahedron42: 3351-3403 (1986)), and as tools for the synthesis of organiccompounds (Wong, C. H., Science 244: 1145-1152 (1989); Chemtracts-Org.Chem. 3: 91-111 (1990); Klibanov, A. M., Ace. Chem. Res. 23: 114-120(1990)).

[0171] In the clinical area, enzymes can be used in extracorporealtherapy, such as hemodialysis and hemofiltration, where the enzymesselectively remove waste and toxic materials (Klein, M. and Langer, R.,Trends in Biotechnology 4: 179-185 (1986)). Enzymes are used in theseareas because they function efficiently as catalysts for a broad rangeof reaction types, at modest temperatures, with substrate specificity,and with stereoselectivity. Nonetheless, there are disadvantagesassociated with the use of soluble enzyme catalysts that limit their usein industrial and laboratory chemical processes (Akiyama et. al.,Chemtech 627-634 (1988)).

[0172] Enzymes are expensive and relatively unstable compared to mostindustrial and laboratory catalysts, even when used in aqueous mediawhere they normally function. Many of the more economically interestingchemical reactions carried out in common practice are incompatible withaqueous media, where, for example, substrates and products are ofteninsoluble or unstable, and where hydrolysis can compete significantly.In addition, the recovery of soluble enzyme catalyst from product andunreacted substrate often requires the application of complicated andexpensive separation technology. Finally, enzymes are difficult to storein a manner that retains their activity and functional integrity, forcommercially reasonable periods of time (months to years) withoutresorting to refrigeration (4° C. to −80° C. to liquid N₂ temperatures),or to maintenance in aqueous solvents of suitable ionic strength, pH,etc. The use of crystallized enzymatic proteins can avoid suchlimitations and is beneficial in medical, clinical, research, andindustrial applications. For instance, the slow dissolution rate ofprotein crystals has been utilized to achieve sustained release ofmedications, such as crystalline formulations of insulin,interferon-alpha, and pancreatic enzymes. (see, e.g., Matsuda, et al.1989 J. Biol. Chem. 264, 13381; Peseta, et al., in Annual Review ofBiochemistry, Vol. 56, edited by Richardson, et al.; Annual Reviews:Palo Alto, 1989; p. 727; Brange, J. in The Galenics of Insulin. Berlin:Springer, 1987; Reichert, et al., Metal-interferon-alpha crystals. U.S.Pat. No. 5,441,734, 1995; Long, et al., Crystal Growth 1996, 168, 233;and reference to the Cross-Linked Enzyme Crystal formulations (CLEC®) ofAltus Biologics Inc. USA).

[0173] Accordingly, the present invention encompasses crystalcompositions of AcpS.

[0174] Such crystals can be produced as described herein or madeaccording to any method in the art such as, e.g., those described inMcPherson, et al. 2000 Annu Rev Biophys Biomol Struct.;29:361-410;McPherson, A 1998. Crystallization of Biological Macromolecules, ColdSpring Harbor Laboratory Press, Cold Spring Harbor, N.Y.; Gilliland, G.L. 1988. A biological macromolecule crystallization database: a basisfor a crystallization strategy. J. Cryst. Growth 90: 51-59; Chernov A.A. 1998 Acta Crystallogr A. Nov 1;54(Pt 6 Pt 1):859-872; McPherson 1985Methods Enzymol. 114:112; and Gilliland 1988 J. Crystal Growth 90:51-59, which include a comprehensive list of suitable conditions inreviews of the crystallization literature. Such an AcpS crystal will beuseful as a composition in medical, clinical, research, industrial andpharmaceutical applications as described herein.

[0175] In another particular embodiment, a crystal composition of thepresent invention is modified by creating an immobilized AcpS crystal ofthe invention, such as, for example, by linking AcpS crystals to eachother and/or to a solid substrate (using any number of linking reagentsand linking methods or linking means known in the art. For example, suchas those described in U.S. Pat. No. 6,004,768; U.S. Pat. No. 6,042,824;WO 01/1638A2; Weygand, et al 2000 J. Mater Chem. 10:141-148; Pum, et al2000 Nanotechnology 11: 100-107; and Ullman, 1991 An Introduction toUltrathin Organic Films: From Langmuir-Blodgett to Self Assembly,Academic Press). Immobilized enzyme crystals retain their catalyticactivity and have improved characteristics such as greater stability andresistance to degradation (see, e.g., S. J.. Bayne et al.,“Enzymatically Active, Cross-Linked Pig Heart Lactate DehydrogenaseCrystals”, Carlsberg Res. Comm., 41, pp. 211-216 (1976); A. Dyer et al.,“A Thermal Investigation of the Stability of Crystalline Cross-LinkedCarboxypeptidase A”, Thermochimica Acta, 8, pp. 455-464 (1974); J. VHupkes, “Practical Process Conditions for the Use of Immobilized GlucoseIsomerase,” Starch, 30, pp. 24-28 (1978); P.J. Kasvinsky et al.,“Activity of Glycogen Phosphorylase in the Crystalline State”, J. Biol.Chem., 251, pp. 6852-6859 (1976); and H. Mrsten et al., “CatalyticActivity of Non-Cross-Linked Microcrystals of Aspartate Aminotransferasein Poly (ethylene glycol)”, Biochem. J., 211, pp. 427-434 (1983)). Suchimmobilized AcpS crystals are also useful as a composition in medical,clinical, research, industrial and pharmaceutical applications asdescribed herein.

[0176] In a more particular embodiment, an immobilized crystalcomposition of the invention is produced by linking an AcpS crystal witha bifunctional linking reagent, such as, for example, glutaraldehyde.This results in the stabilization of the crystal lattice contactsbetween the individual enzyme catalyst molecules constituting thecrystal. As a result, the crystals are immobilized and function atelevated temperatures, extremes of pH and in harsh aqueous, organic, ornear-anhydrous media, including combinations of such conditions.Therefore, in one embodiment, an immobilized crystal composition of theinvention functions in environments incompatible with the functionalintegrity of corresponding uncrystallized, unimmobilized, and/or itscorresponding enzyme in the native state.

[0177] In still further embodiments, immobilization of an AcpS crystalfurther encompasses without limitation, an AcpS crystal of the inventionbeing: caged (such as, e.g., Schnur, J. M. 1993. Lipid tubules: Aparadigm for molecularly engineered structures. Science 262: 1669-1676;Schnur, et al. 1994. Biologically engineeredmicrostructures—controlled-release applications. J. Controlled Release28 (1-3)(Jan.): 3-13); encapsulated (such as, e.g., in foams, fluids,gels, polymers or membranes see, e.g., WO 00/18972AD; WO 98/23734);tethered (such as, e.g., by an antibody or antibody binding fragment);coupled; bound to bacterial S-layers in predictable and geometricallywell defined ways (see, e.g., Pum & Sleytr 1999 Trends in Biotechnology17:8-11 and the references cited therein); coated (such as, e.g., withnanoparticles or polyelectrolyte molecules); electrostatically bound;layered; (such as, e.g., in 2D crystal arrangements); formed by placingAcpS proteins beneath lipid monolayers then subsequently stabilized intoa durable geometric arrangement; covalently, or non-covalently bondedusing any method in the art (such as, e.g., WO 00/77281 Al; U.S. Pat.No. 5,091,187; U.S. Pat. No. 5,716,709; McPherson, A 1998.Crystallization of Biological Macromolecules, Cold Spring HarborLaboratory Press, Cold Spring Harbor, N.Y. or; Gilliland, G. L. 1988. Abiological macromolecule crystallization database: a basis for acrystallization strategy. J. Cryst. Growth 90: 51-59; Sára, et al. 1996in Crystalline Bacterial Cell Surface Proteins (Sleytr, et al. Eds), pp.133-159, R. G. Landesall).

[0178] Immobilized AcpS crystals can be lyophilized, producing AcpScompositions which can be stored at non-refrigerated (room) temperaturesfor extended periods of time, and which can be reconstituted in aqueous,organic, or mixed aqueous organic solvents of choice, without theformation of amorphous suspensions and with minimal risk ofdenaturation. The lyophilization of such resulting compositions providesa means of improving storage, handling, and manipulation properties ofAcpS crystals of the invention. Use of the term “AcpS crystal” hereinencompasses both immobilized and unimmobilized forms as described hereinunless the context would clearly dictate otherwise to one skilled in theart to which it applies.

[0179] Using such crystal compositions, the present invention alsoencompasses methods of making selected products with them. For example,in the research and pharmaceutical area, AcpS crystals can be used inthe preparation of acyl-carrier proteins (ACP) or ACP analogs or ACPderivatives such as, for example, ACP analogs with modifiedphosphopantetheines (see, e.g., Gehring, et al., 1997 “Ability ofStreptomyces Acyl Carrier Proteins and Coenzyme A Analogs to Serve asSubstrates in vitro for E. coli holo-ACP Synthase” in Chemistry andBiology 4:17). ACP analogs can be used to probe mechanistic questions inenzymes involved in the biosynthesis of fatty acids and they can also beused for commercial or pharmaceutical applications, such as, e.g., tofacilitate the production of polyketides and polyketide derivatives,which have been shown to have many useful functions (for example, e.g.,the polyketide antibiotic erythromycin A is used against Gram-positivebacterial infections, particularly against penicillin-resistantinfections. Another polyketide, Amphotericin-B, is used primarily as anantifungal agent. The tetracyclines are broad-spectrum antibioticpolyketides that have activity against both Gram-positive andGram-negative bacteria. Another important polyketide is doxorubicin(also known as Adriamycin), which is a widely used antitumor agent,particularly against solid tumors. Further, another interestingcomposition is the polyketide derivative lovastatin, a compound that hasfound wide use as a cholesterol reducing agent under the trade name ofMevacor®). Due to the broad substrate specificity of the AcpS enzyme,AcpS crystals themselves can also be used in the production ofpharmaceutical reagents such as the above mentioned polyketides (see,e.g., Suo, et al. 2001 Proc Natl Acad Sci U S A 98(1):99-104).Accordingly, AcpS crystalline compositions are useful in the manufactureor catalysis of selected products such as for research, pharmaceutical,or industrial applications.

[0180] AcpS Crystalline Compositions for Use in Microelectronics

[0181] In still another embodiment, an AcpS crystal of the invention canbe used, for example, as a fabrication material in the process,manufacture, and/or production of a microelectronic device. In oneembodiment, AcpS protein crystals are employed using saturated solutionsin the formation of a two-dimensional (2D) crystalline array on a solidsupport (such as, e.g., a silicon wafer). In 2D-nucleation growth, a 2Disland is first nucleated on a flat crystal face. The 2d crystal islandis a collection of molecules that are usually a single growth layer inheight. Such an application of a crystal of the invention is useful as,for example, a nanometre-thick resist in semiconductor technologies andas a template for the formation of regularly arranged nanoparticles forapplications in molecular electronics (see, e.g., Share, et al. Gradientcomposite replicas from protein crystal layer templates produced bypulsed laser deposition. PTB-Berichete, F-39, pp. 8-16; “BiologicallyDerived Nanometer-Scale Patterning on Chemically Modified SiliconSurfaces,” B. W. Holland, K. Douglas, N. A. Clark, Mat. Res. Soc. Symp.Proc. 330, 121 (1994); “Transfer of Biologically-Derived Nanometer-ScalePatterns to Smooth Substrates,” K. Douglas, G. Devaud, N. A. Clark,Science 257, 642 (1992); Abstract Y13.14 Laser Seeding for BiomolecularCrystallization Bancel, et al., from the 1998 March Meeting of TheAmerican Physical Society Los Angeles, Calif. showing a novel seedingtechnique in which a laser beam is used to select and transfermicroscopic seed crystals in a growth solution; Allara, D. L. 1996.Nanoscale structures engineered by molecular self-assembly offunctionalized monolayers. In Nanofabrication and Biosystems. Ed. H. C.Hoch, L. W. Jelinski, and H. G. Craighead. New York: CambridgeUniversity Press, U.S. Pat. No. 5,597,457; WO 01/16328 for theapplication of proteins to a substrate. Additional references can befound in the work of Whitesides and colleagues which is described andreferenced in WO 97/06468 and in the following patents: WO9954786 (A1)Elastomeric mask and use in fabrication of devices, including pixelatedelectroluminescent displays; WO9629629 (A2, A3), Microcontact printingon surfaces and derivative articles; W09707429 (A1), Self-assembledmonolayer directed patterning of surfaces; WO9858967 (A1),Self-assembling peptide surfaces for cell patterning and interactions;U.S. Pat. No. 6,197,515, Molecular recognition at surfaces derivatizedwith self-assembled monolayers; U.S. Pat. No. 6,180,239, Microcontactprinting on surfaces and derivative articles; U.S. Pat. No. 5,976,826,Device containing cytophilic islands that adhere cells separated bycytophobic regions; U.S. Pat. No. 5,900,160, Methods of etching articlesvia microcontact printing; U.S. Pat. No. 5,512,131, Formation ofmicrostamped patterns on surfaces and derivative articles; U.S. Pat. No.5,620,850, Molecular recognition at surfaces derivatized withself-assembled monolayers; U.S. Pat. No. 5,776,748, Method of formationof microstamped patterns on plates for adhesion of cells and otherbiological materials, devices and uses therefor.).

[0182] One advantage of using an AcpS crystal in microfabrication and inmicrolithography is that it permits the design and realization ofsmaller transistors that can be fabricated on a computer chip. Reductionin transistor size permits greater numbers of transistors in a definedarea and thus faster data processing times that use less energy. Suchreductions in transistor size support “Moore's Law,” which describes apredictable and continuing trend in the development of memory chipperformance so that each new computer memory chip contains roughly twiceas much capacity as its predecessor. Use of AcpS crystals in microchipfabrication provides another method for realizing “Moore's Law.”

[0183] Methods of fabricating microchips using proteins such as the AcpScrystals of the invention can be accomplished without undueexperimentation using any known method in the art of protein engineeringand microlithography. For example, one technique used in micro- andnanoelectronic applications is a microlithographic procedure using deepultraviolet (DUV) laser irradiation for transferring (sub) micrometerpatterns on a substrate to pattern 2D protein layers on silicon wafers(see, e.g., Pum, et al. 1996 Colloids Surf. B: Biointerfaces 8, 157-162;Pum, D. et al. 1997 Microelectron. Eng. 35, 297-300; and Calvert, J. M.1993 J. Vaccine Sci. Technol. B 11, 2155-2163 and Pum & Sleytr 1999Trends in Biotechnology 17:8-11). Typically, patterns are formed on 2Dlayers by bringing a chromium mask (on quartz glass) into direct contactwith the 2D protein crystal layer on a silicon wafer. Upon irradiationwith ArF pulses (DUV emitted after excitation of argon-fluoride gas inan excimer laser; wavelength 193 nm, dose ˜100 mJ per squared cm, pulseduration ˜8 nsec), the protein layer is completely removed in theexposed areas (i.e. without the mask) but retains its structural andfunctional integrity in the unexposed regions (i.e. masked areas). Themasked or unexposed regions can subsequently be used to selectively bindother biologically functional molecules (here, for example, such as AcpSto form an AcpS/apo-ACP binding complex) or to be reinforced forsubsequent reactive ion etching using any techniques in the art.Different etching rates between exposed and unexposed regions arenecessary for reactive-ion etching and can obtained by reinforcing theprotein layer (here, the AcpS layer) with silicon, a procedure known assilylation (see, e.g., Shaw, et al. 1989 J. Vaccine Sci. Technol. B 7,1709). Using similar techniques, crystal protein layers are currentlybeing produced for use as novel high-performance resists with thicknessin the 10 nm range (see, e.g., Pum & Sleytr 1998 in Biological MoleculesIn Nanotechnology: The Convergence of Biolechnology, Polymer Chemistryand Materials Science, IBC Library Series pp.139-143 Southborough:International Business Communication, Inc.; Pum, et al. 1996 ColloidsSurf. B: Biointerfaces 8, 157-162; WO 01/16328 Pum, et al. 1997Microelectron. Eng. 35, 297-300).

[0184] Using these and similar techniques, one of skill in the art coulduse an AcpS crystal of the invention to serve as a fabrication maskand/or a template for improvements in silicon nano- andmicro-fabrication technology. This is especially true in light of therecent successes in immobilizing biological nanoparticles (e.g.,enzymes, antibodies, etc.) on these surfaces, leading to functionaldevices that can be employed as sensors, nanoelectrodes, prostheticdevices, or nanomachines.

[0185] AcpS Crystalline Compositions for Use in Biosensors

[0186] In another embodiment, a crystal composition of the invention isemployed as a biomaterial for use in a biosensor. Biosensors usebiomaterials, such as, e.g., an AcpS crystal of the application, todetect various substances of clinical, industrial, and other interest(see, e.g., Hall, E., Biosensors, Open University Press (1990)).

[0187] Biomaterials, such as those comprising a crystal of the invention(fabricated as described herein), can be integrated with a solid supportusing any number of strategies such as, e.g., those previously describedherein and the following:

[0188] (1) by incorporation in organic or inorganic polymers that areassociated with the solid matrices (see, e.g., Cosnier, S. (1997)Electropolymerization of amphiphilic monomers for designing amperometricbiosensors. Electroanal. 9, 894-902; Kranz, C. et al. (1998) Controlledelectrochemical preparation of amperometric biosensors based onconducting polymer multilayers. Electroanal. 10, 546-552; Willner, I. etal. (1992) Bioelectrocatalyzed reduction of nitrate utilizingpolythiophene bipyridinium enzyme-electrodes. Bioelectrochem. Bioenerg.29, 2945; Heller, A. (1992) Electrical connection of enzyme redoxcenters to electrodes. J. Phys. Chem. 96, 3579-3587; Gregg, B. A. andHeller, A. (1990) Cross-linked redox gels containing glucose-oxidase foramperometric biosensor applications. Anal. Chem. 62, 258-263; Gregg, B.A. and Heller, A. (1991) Redox polymer-films containing enzymes. 1. Aredox-conducting epoxy cement—synthesis, characterization andelectrocatalytic oxidation of hydroquinone. J. Phys. Chem. 95,5970-5975; Gregg, B. A. and Heller, A. (1991) Redox polymer-filmscontaining enzymes. 2. Glucose-oxidase containing enzyme electrodes. J.Phys. Chem. 95, 5976-5980; Walcarius, A. (1998) Analytical applicationsof silica-modified electrodes—a comprehensive review. Electroanal. 10,1217-1235; Tsionsky, M. et al. (1994) Sol-gel-derived ceramic carboncomposite electrodes—introduction and scope of applications. Anal. Chem.66, 1747-1753);

[0189] (2) by the generation of physical blend composites between abiomaterial and an electronic element material (see, e.g., Wang, J. andNaser, N. (1994) Improved performance of carbon-paste amperometricbiosensors through the incorporation of fumed silica. Electroanal. 6,571-575; Hale, P. D. et al. (1991) Amperometric glucose biosensors basedon redox polymer-mediated electron-transfer. Anal. Chem. 63, 677-682;Hale, P. D. et al. (1989) A new class of amperometric biosensorincorporating a polymeric electron-transfer mediator. J. Am. Chem. Soc.111, 3482-3484; Kaku, T. et al. (1994) Amperometric glucose sensorsbased on immobilized glucose oxidase polyquinone system. Anal. Chem. 66,1231-1235) e.g. redox enzymes in carbon paste blends); or

[0190] (3) by the incorporation of biomaterials in membrane assembliesorganized on the transducers (Kinnear, K. T. and Monbouquette, H. G.(1993) Direct electron-transfer to Escherichia coli fumarate reductasein self-assembled alkanethiol monolayers on gold electrodes. Langmuir2255-2257).

[0191] The functionalization of solid supports with monolayers,multilayers of controlled thickness, or thin film assemblies ofbiomaterials, reveals several attractive features for bioelectronicdevices such as biosensors. Besides the fundamental feasibilities tostructurally control, manipulate and address biomaterials such asprotein crystals in 2D or thin 3D crystal arrays, these configurationsexhibit practical advantages because they lack diffusional barriers, andbiological processes that occur on the surface are rapidly translated toelectronic outputs of a biosensor. The chemistry of surface modificationof solid interfaces for use with monolayer and multilayer arrays hasbeen addressed in several comprehensive review articles (see, e.g.,Langmuir 2255-2257; Albery, W. J. and Hillman, A. R. (1982). Modifiedelectrodes. Annu. Rep. Prog. Chem. Sect. C 78, 377-437; Murray, R. W.(1984) Chemically modified electrodes. In Electroanalytical Chemistry(Vol. 13) (Bard, A. J., ed.), pp. 191-368, Marcel Dekker, New York;Wrighton, M. S. (1986) Surface functionalization of electrodes withmolecular reagents. Science 231, 32-37; Finklea, H. O. (1966)Electrochemistry of organized monolayers of thiols and related moleculeson electrodes. In Electroanalytical Chemistry (Vol. 19) (Bard, A. J. andRubinstein, I., eds), pp. 109-335, Marcel Dekker, New York; Zhong, C. J.and Porter, M. D. (1995) Designing interfaces at the molecular level.Anal. Chem. 67, 709A-715A.

[0192] For example, functionalized thiolate monolayers associated withgold electrodes have been used as base interfaces for the covalentlinkage of biomaterials, for example, enzymes (Shoham, B. et al. (1995)A bilirubin biosensor based on a multilayer network enzyme electrode.Biosens. Bioelectron. 10, 341-352; Riklin, A. and Willner, I. (1995)Glucose and acetylcholine sensing multilayer enzyme electrodes ofcontrolled enzyme layer thickness. Anal. Chem. 67, 4118-4126) orantibodies (Cohen, Y. et al. (1996) Modified monolayer electrodes forelectrochemical and piezoelectric analysis of substrate-receptorinteractions; novel immunosensor electrodes. J. Electroanal. Chem. 417,65-75). Alternatively, functionalized siloxane films immobilized ontooxide solid supports can be used to assemble biomaterials on the oxidesurfaces (Zou, C. F. and Wrighton, M. S. (1990) Synthesis ofoctamethylferrocene derivatives via reaction of(octamethylferrocenyl)methyl carbocation with nucleophiles andapplication to functionalization of surfaces. J. Am. Chem. Soc. 112,7578-7584; Murray, R. W. (1980) Chemical modified electrodes. Acc. Chem.Res. 13, 135-141; Abruña, H. D. (1998) Coordination chemistry in 2dimensions - chemically modified electrodes. Coord. Chem. Rev. 86,135-189).

[0193] Using such teachings and knowledge in the art, one of ordinaryskill could use a crystal composition of the invention as a biomaterialof a biosensor, for use in detecting and/or quantitating an analyte ofinterest, such as an analyte in a fluid, such as, for example abiological sample (e.g., a bodily fluid, such as, e.g., blood, urine,lavage, sputum, etc.), chemical and laboratory reaction media, organicmedia, water, culture media, foodstuffs, and beverages. In someinstances, the fluid in question can be a gas.

[0194] In one particular embodiment, an AcpS crystal is used as abiomaterial in a biosensor and brought into contact with a fluid todetect an analyte. The analyte can be measured directly (such as, e.g.,blood glucose level) or indirectly (e.g., such as by detecting orquantitating a substance which is a reactant (product or substrate) in areaction in which the analyte of interest participates. In either case,the crystal composition is able to interact with the analyte or asubstance that is a reactant in a reaction (such as, e.g., ananalyte-binding partner that forms a binding complex with an AcpScrystal composition) in which the analyte also participates. Theinteraction of a crystal form of the enzyme of the invention with ananalyte results in a detectable change such as, e.g., any of thefollowing non-limiting examples: a change in pH; a colormetric change; aproduction of reaction product; a weight change; a change in aninterference pattern (such as an interference pattern produced by areflected wave, such as, e.g., a wave of light, a photon, a sound wave,a pressure wave, etc.); the production of light; a piezoelectric effect;a change in conductivity (such as, e.g., conductivity of: heat, light,ionic, electric, gravimetric, etc.); a change in heat; a change inelectrical potential. Any such change detected and/or quantitated by anyappropriate detecting means such as, e.g., without limitation: a pHelectrode, a light or a heat sensing device, a means for measuring aninterference pattern (e.g., such as a means for analyzing aninterference pattern produced by coherent light), a means for measuringa fluctuation in weight; a means for measuring an enzymatic assay; agravimetric detecting means; a means for measuring electrical charge;and/or a means for detecting a formation of an enzyme/binding partnercomplex is also encompassed herein. Any means useful for detecting achange resulting from an enzyme interaction with an analyte can be usedand is encompassed by the present application. Typically a biosensor ofthe present invention comprises a crystal AcpS composition and aretaining means for the crystal which allows contact between thecrystal(s) and an analyte of interest or a substance in a sample (e.g.,such as a biological, organic, or inorganic sample) to produce adetectable change, such as, e.g., a change which is a reaction in whichthe analyte of interest participates.

[0195] In a more particular embodiment, a biosensor of the inventioncomprises amperometric detection of binding of an analyte, such as abinding agent, to a crystal composition of the invention (such as, e.g.,a biomaterial comprising a 2D crystalline protein formation or a thin 3Dcrystal array). In this embodiment, the biosensor surface is anelectrode, and the biomaterial is sufficiently closely packed andordered (such as, e.g., in thin layer) to form an effective barrier to acurrent (across the biomaterial) mediated by, for example, a redox ionspecies in an aqueous solution in contact with the biomaterial layer.Binding of a binding agent to the biomaterial, e.g., the 2D crystallineprotein formation or a or thin 3D crystal array, is sufficient to affectcurrent flow (such as, e.g., current flow mediated by a redox species)so that binding to a crystal causes a shape change (such as, e.g.,through cracking of the crystal and/or by shifting the order of thecrystal packing), which subsequently permits a change in current flowacross or through the biomaterial. In one such embodiment, a chamber inan apparatus is adapted to contain an aqueous solution of redox speciesin contact with a layer of a crystal of the invention, and the detectorincludes a circuit for measuring ion-mediated current across the layerin response to a binding event occurring between an AcpS crystalcomposition and an anaylate to form a binding complex with said crystal.The triggering event in such a biosensor is the binding of an anaylateto the AcpS crystal. Without being bound by theory, this binding canperturb the ordered structure of the biomaterial layer (or a sufficientnumber of individual crystals) to permit movement of redox speciesthrough the biomaterial to produce a detectable current or currentchange. In one example, the biosensor detects a binding event as anincrease or decrease in current across an electrode, i.e., betweenworking and counter electrodes. By analogy to a transistor, the redoxsolution serves as a “source,” the biomaterial layer as a “gate,” andthe underlying electrode as the “drain.” Current in the biosensor“transistor” is initiated by applying a threshold voltage to the gate.In this embodiment, current is initiated by a stimulus to the monolayer“gate,” i.e., by binding to a crystal.

[0196] One extant example of an amperometric biosensor uses glucoseoxidase modified with a ferrocene conductor. The modified enzyme isself-assembled onto a porous gold-black electrode to detect glucose insolution by exploiting an electron transfer pathway of the enzyme as asensor (Aizawa, et al., 1996. Molecular assembly technology forbiosensors. In Nanofabrication and Biosystems: Integrating MaterialsScience, Engineering And Biology. Ed. Hoch, et al., New York: CambridgeUniversity Press).

[0197] In another embodiment, a biosensor is designed for gravimetricdetection of binding of a binding agent to a crystal of the invention.In such an embodiment, the biosensor surface is a piezoelectric AcpScrystal.

[0198] The detector functions by generating a surface acoustic wave inthe crystal and then detecting a shift in wave frequency, velocity, orresonance frequency of a surface acoustic wave produced in response to abinding event occurring between the crystal and an anaylate forming abinding complex with said crystal. Surface acoustic waves are generatedin the crystal or crystal layer by any oscillator means. Not being boundby theory, but, according to currently accepted piezoelectricprinciples, the change in mass of the biomaterial resulting from bindingof an AcpS crystal alters the frequency, resonance frequency, and/orwavelength of the surface acoustic waves, and at least one of these wavecharacteristics is measured by a detector means. The oscillator anddetector collectively form a detector means for detecting binding of abinding agent to an AcpS crystal on the biosensor surface. Details ofassociated detector means in gravimetric biosensors are given, forexample, in U.S. Pat. Nos. 5,478,756 and 4,789,804, and in PCTapplication WO 96/02830.

[0199] In still another embodiment, a biosensor encompassed herein isdesigned for optical surface plasmon resonance (SPR) detection ofbinding of a binding agent to a crystal composition of the invention. Inthis embodiment, the biosensor surface is a transparent dielectricsubstrate coated with a thin metal layer on which a 2D crystal layer orthin 3D crystal composition layer of the invention is formed so that thesubstrate and metal layer form a plasmon resonance interface. Thedetector functions to excite surface plasmons at a plasmon resonanceangle which is dependent on the optical properties of the metal film andattached biomaterial layer, and to detect a shift in plasmon resonanceangle in response to a binding event occurring between a crystalcomposition and an anaylate to form a binding complex.

[0200] Typical elements of a surface plasmon resonance (SPR) biosensorcomprise: an open-top chamber in the biosensor which contains awaveguide composed of a dielectric film and a thin evaporated metal filmconstructed to support surface plasmon waves at the dielectric/metalfilm interface. The waveguide surface forms a biosensor surface having acrystal layer (such as, e.g., a crystalline 2D layer of AcpS or otherfinally deposited crystalline AcpS biomaterial). A light sourcedirecting a divergent light beam onto the biosensor surface through alens. At some region along the length of the biosensor surface, the beamangle strikes the surface at an absorption angle at which absorptionfrom the evanescent wave by surface plasmons occurs. The absorptionangle will shift with changes in the composition of the biomaterial nearthe interface, that is, in response to binding events occurring at thecrystal surface. The intensity of reflected light from each region alongthe biosensor surface is monitored by a photosensor whose photosensinggrid is matched to specific detector surface regions, and which isoperatively connected to an analyzer means. The light source andphotosensor in this embodiment are referred to herein as biosensormeans. In operation, the SPR absorption angle on the surface of thebiomaterial is measured before and after addition of an analyte, withthe measured shift in angle being proportional to the extent of bindingof an analyte to form an AcpS/binding partner complex.

[0201] In an additional embodiment, a biosensor encompassed by theinvention employs optical detection of binding of a binding agent to acrystal of the invention. The optical detector functions by irradiatinga biomaterial surface of the biosensor with a light beam (such as, e.g.,coherent light) and then detecting a change in the optical properties ofthe biomaterial. In one example, the detecting means uses ellipsometry(an optical physical measurement technique which can be used to measuresmall changes of refraction index at surfaces with high sensitivity, bymeasuring changes in elliptisity of polarized light, such as thosecaused by the presence of analyte biomolecules on the surface of abiomaterial of the invention) to detect binding.

[0202] Such biosensor applications can be used herein with a crystalcomposition of the present invention. More specifically, crystallizedAcpS can be used in a biosensor application as described to detect thepresence of a pathogen, such as e.g., but without limitation, the abacterial or fungal agent that can cause a disease, disorder, condition,syndrome, or symptom such as, e.g., the following agents: Gram-Negativeand Gram-positive bacteria and bacterial families and fungi such as:Actinomycetales (e.g., Corynebacterium, Mycobacterium, Norcardia),Cryptococcus neoformans, Aspergillosis, Bacillaceae (e.g., Anthrax,Clostridium), Bacteroidaceae, Blastomycosis, Bordetella, Borrelia (e.g.,Borrelia burgdorferi), Brucellosis, Candidiasis,Campylobacter,Coccidioidomycosis, Cryptococcosis, Dermiatocycoses, E.coli (e.g., Enterotoxigenic E. coli and Enterohemorrhagic E. coli),Enterobacteriaceae (Klebsiella, Salmonella (e.g., Salmonella typhi, andSalmonella paratyphi), Serratia, Yersinia), Erysipelothrix,Helicobacter, Legionellosis, Leptospirosis, Listeria, Mycoplasmatales,Mycobacterium leprae, Vibrio cholerae, Neisseriaceae (e.g.,Acinetobacter, Gonorrhea, Menigococcal), Meisseria meningitidis,Pasteurellacea Infections (e.g., Actinobacillus, Heamophilus (e.g.,Heamophilus influenza type B), Pasteurella), Pseudomonas,Rickettsiaceae, Chlamydiaceae, Syphilis, Shigella spp., Staphylococcal,Meningiococcal, Pneumococcal and Streptococcal (e.g., S. typhimurium,Streptococcus pneumoniae and Group B Streptococcus).

[0203] For example, it has been shown that during infections AcpSproteins are specifically upregulated (e.g., the fadB gene of S.typhimurium (which encodes AcpS I) was identified in a screen for genesexpressed during infection using in vivo expression technology (Mahan,et al. 1995 Proc Natl Acad Sci USA 92:669-673; and Mahan, et al. 1993Infect Agents Dis 2:263-268) and the fadF gene also of S. typhimurium(which encodes AcpS II) was induced after the bacteria wasphagocytosised by macrophages (DiRusso, et al. 1999 Progress in LipidResearch 38:129-197)). Accordingly, biological samples comprising aninfectious agent and/or constituents thereof could be applied to abiosensor on a microchip for analytical, quantitative, and/orqualitative chemical analysis. Such “lab-on-a-chip” functions can beused for example, to determine the presence or level (compared to acontrol) of CoA and/or apo-ACP in a sample thus indicating the presenceof an infectious agent. In another embodiment, AcpS crystals are used ina biosensor to determine binding agents that can modify an AcpSactivity, for example, such as by acting as an agonist or antagonist.

[0204] Further embodiments of the present invention includecomputer-readable media encoded with data representing the atomiccoordinates of the three-dimensional structure of Streptococcuspneumoniae AcpS, or computer-readable media having stored thereon amodel comprising the three-dimensional structure of the catalytic activesite domain of Streptococcus pneumoniae AcpS. As used herein, the term“computer-readable medium” refers to any medium that can be read andaccessed directly by a computer. Such media include, but are not limitedto, magnetic storage media, such as floppy discs, hard disc storagemedia, and magnetic tape; optical storage media, such as optical discsor CD-ROMs; electrical storage media, such as RAM and ROM; and hybridsof these categories, such as magnetic/optical storage media. Those ofordinary skill in the art can readily appreciate how any of thepresently known computer-readable media can be used to create amanufacture comprising a computer-readable medium having recordedthereon an amino acid or nucleotide sequence and/or atomic coordinatesof the present invention.

[0205] Other features of the present invention will become apparent fromthe following examples, which are for illustrative purposes only, andwhich are not intended to limit the invention in any way.

EXAMPLE 1 Cloning of the S. pneumoniae acpS and acpP Genes; Expressionand Purification of ACPS and ACPP

[0206] To understand better the function of AcpS in Streptococcuspneumoniae, a sphere-shaped, Gram-positive bacterium and major humanpathogen of the upper respiratory tract, and to explore AcpS as anantibacterial target, the acpS and acpP genes of S. pneumoniae arecloned and expressed, and the gene products characterized. As disclosedbelow, the results disclosed herein demonstrate that S. pneumoniae AcpSshares many biochemical properties with E. coli AcpS. In addition, theresults suggest that AcpS proceeds by an ordered reaction mechanism withthe initial formation of the enzyme-apo-ACP intermediate from apo-ACP,followed by the transfer of 4′-phosphopantetheine from CoA to theapo-ACP of the complex. Finally, both acpS and acpP form complex operonswith the genes whose functions are not required for fatty acidbiosynthesis.

[0207] AcpS, an enzyme essential for bacterial fatty acid synthesis,catalyzes the transfer of 4′-phosphopantetheine from CoA to apo-ACP toform holo-ACP along with the production of 3′,5′-ADP, and is anattractive target for the development of antibacterial drugs. Thestructure of AcpS reveals an α/β fold, and demonstrates that thetrimeric structure of the enzyme appears to be essential for the AcpSactivity. These results represent the first structural determination ofthe interaction between the AcpS enzyme and its product, 3′,5′-ADP.These data provide a starting point for structure-based drug designefforts that should identify novel AcpS inhibitors with potentantibacterial activity.

[0208] To solve the structure of the S. pneumoniae AcpS, the protein ispurified to homogeneity from an E. coli expression host using athree-step purification method (McAllister et al., 2000). The purifiedAcpS is crystallized as described below. Crystals of AcpS are obtainedafter 4-5 days at room temperature. Data are collected from thesecrystals, and the structure of AcpS is then solved by the multipleanomalous dispersion method (Hendrickson et al., 1991) (MAD) usingselenomethionine-substituted protein and exploiting non-crystallographic3-fold averaging.

[0209] Materials

[0210] Unless specified otherwise, all fine chemicals are from SigmaChemical Company (St. Louis, Mo.). All fast protein liquidchromatography (FPLC) resins and columns used for protein purification,and strains and reagents for construction, expression, and purificationof GST-fused proteins, are obtained from Amersham Pharmacia Biotech(Piscataway, N.J.). Luria Bertani (LB) broth medium is purchased fromBio101, Inc. (Vista, Calif.). All polyacrylamide gels and reagents arepurchased from Novex (San Diego, Calif.). SYPRO Orange and Bradfordprotein assay reagents are purchased from BIO-RAD (Hercules, Calif.),and Sulfo-EGS (ethylene glycolbis(succinimidylsuccinate)) is obtainedfrom Pierce (Rockford, Ill.). ³H-CoA (specific activity, 1.5 Ci/mmol) iscustom-synthesized by NEN Life Science Products (Boston, Mass.).

Cloning and Expression of the acpS and acpP Genes of S. pneumoniae(hex-) R6

[0211] The acpS and acpP genes are cloned from S. pneumoniae by PCRusing the same reagents, plasmids, and cell lines used for cloning andexpression as described in Zhao et al., 1999. The sequences of the S.pneumoniae acpS gene and AcpS protein are disclosed in U.S. Pat. No.6,060,282, issued May 9, 2000 (note also GenBank accession numberAF276617). The acpS gene, 369 bp long, encodes a protein consisting of122 amino acid residues, with a predicted molecular weight of 13.7 kDa(accession number AF276617). As disclosed in this patent, the deducedamino acid sequence of the S. pneumoniae AcpS protein consists of 122amino acids, as follows (SEQ ID NO:1): Met Arg Met Ile Val Gly His GlyIle Asp Ile Glu Glu Leu Ala Ser Ile Glu Ser Ala Val Thr Arg His Glu GlyPhe Ala Lys Arg Val Leu Thr Ala Gln Glu Met Glu Arg Phe Thr Ser Leu LysGly Arg Arg Gln Ile Glu Tyr Leu Ala Gly Arg Trp Ser Ala Lys Glu Ala PheSer Lys Ala Met Gly Thr Gly Ile Ser Lys Leu Gly Phe Gln Asp Leu Glu ValLeu Asn Asn Glu Arg Gly Ala Pro Tyr Phe Ser Gln Ala Pro Phe Ser Gly LysIle Trp Leu Ser Ile Ser His Thr Asp Gln Phe Val Thr Ala Ser Val Ile LeuGlu Glu Asn His Glu Ser

[0212] It is not known if the AcpS protein as naturally produced by S.pneumoniae begins with Met Arg or Met Ile. For the purpose of thestudies herein, a primer corresponding to the second Met start codon atthe N-terminus of the foregoing sequence is designed and used forcloning the S. pneumoniae acpS gene. Thus, the acpS coding sequence usedfor expression of the protein herein produces an AcpS protein lackingthe first two amino acid residues (Met Arg) of the foregoing sequence.Specifically, the following PCR primers are designed and used to amplifythe acpS gene for cloning into E. coli expression systems. The 5′ PCRprimer (5′-CGCGGATCCCATATGATAGTTGGACACGGAATTG -3′; SEQ ID NO:2) isdesigned at the second ATG start codon of acpS, and contains BamHI andNdeI sites for cloning purposes. The 3′ PCR primer(5′-CGCGGATCCCTAGCTTTCATGAATTTCCTCC -3′; SEQ ID NO:3) is designed at thestop codon of acpS, and contains a BamHI site after the stop codon.Using these primers, acpS is PCR amplified from S. pneumoniae for 25cycles under the conditions described in Zhao et al., 1999. Five PCRreaction products are combined, and a portion of the pooled PCR productsis digested with BamHI. The BamHI-digested PCR fragment is cloned intopCZA342, a low copy number plasmid (Baltz et al., 1997) that is digestedwith BamHI and dephosphorylated with calf intestinal alkalinephosphatase. acpS from several pCZA342 clones is sequenced, and a clonecontaining the consensus acpS gene sequence is used for constructingexpression systems. This pCZA342 clone is digested with NdeI and BamHI.The NdeI-BamHI DNA fragment containing acpS is subcloned into pET-11a(Novagen). The resulting construct is designated as pRBP-19. The pCZA342clone is also digested with BamHI, and the BamHI fragment of acpS issubcloned into pGEX-2T, resulting in pRBP-20.

[0213] To clone the acpP gene, the following PCR primers are used foramplification. 5′ PCR primer:

[0214] 5′-CGCGGATCCCATATGACAGAAAAAGAAATTTTTGACCGTATTG -3′ (SEQ ID NO:4);3′ PCR primer:

[0215] 5′-CGCGGATCCGAATTCCTATTTTCCTTGAATGATTTTAACCACATC-3′ (SEQ IDNO:5). Using these primers, acpP is PCR amplified from S. pneumoniae asdescribed above. The PCR products are digested with BamHI. TheBamHI-digested PCR fragment is cloned into pCZA342. The pCZA342 clone isdigested with NdeI and BamHI. The NdeI-BamHI DNA fragment containingacpP is subcloned into pET-11a (Novagen), resulting in pRBP-16.

[0216] Purification of AcPS and ACP of S. pneumoniae

[0217] LY128 (E. coli BL21 (pLysS)/pRBP-19) is first grown at 35° C.overnight in LB broth medium supplemented with 100 μg/ml ampicillin. Theovernight culture (40 ml) is then inoculated into 1000 ml of LB mediumsupplemented with ampicillin, and grown at 33° C. with shaking at 250rpm until an OD590 of 0.5-0.6 is reached. The culture is induced with 1mM isopropyl-1-thio-β-D-galactopyranoside (IPTG) for 3 hr. Cells areharvested by centrifugation at 4500×g at 4° C. for 8 min, washed twicein phosphate buffered saline (PBS), resuspended in 50 mM citratephosphate pH 6.0, and disrupted by passing twice through a Frenchpressure cell. The resulting cell extract is centrifuged at 160,000×gfor 40 min at 4° C. The supernatant fraction is collected and applied toa 15S Source S cation exchange column (2.5×8 cm) equilibrated with 50 mMcitrate phosphate, pH 6.0 (buffer A). The column is washed with bufferA, and eluted with a linear gradient of 0-1.0M KCl in buffer A.Fractions (7 ml each) are collected. The presence of AcpS in thefractions is detected by SDS-PAGE analysis (16% tricine gels) (Laemmli,1970). The fractions containing AcpS are pooled, and applied to an S-100Sepharose preparative gel filtration fast protein liquid chromatographycolumn (5.0×60 cm) equilibrated with 50 mM Tris-HCl, pH 7.0, 100 mM KCl.The fractions containing AcpS are collected, adjusted with glycerol to afinal concentration of 15% (v/v), and stored in small aliquots at −70°C. Protein concentration is determined using a protein assay kit(Bio-Rad), with BSA as a standard (Bradford, 1976).

[0218] LY135 (E. coli XL1 Blue (mRF′)/pRBP-20) is grown, induced,harvested, disrupted, and centrifuged as above. The supernatant fractionis applied to a glutathione Sepharose 4B column (10 ml) equilibratedwith 100 ml of PBS. The column is washed with 100 ml of PBS, and theGST-AcpS fusion protein is eluted with 10 mM glutathione in PBS.Fractions are analyzed by SDS-PAGE (12% glycine) and those fractionscontaining GST-AcpS are pooled, dialyzed against 50 mM Tris-HCl, pH 7.0(4 liters), adjusted with glycerol to the final concentration of 15%(v/v), and stored at −70° C. as described above.

[0219] LY140 (E. coli BL21 (pLysS)/pRBP-16) is grown, induced,harvested, and disrupted as described above. The resulting cell extractis also centrifuged as described above. The supernatant fraction iscollected and applied to a 15S Source Q-column (2.5×8 cm) equilibratedwith 50 mM Tris-HCl, pH 8.0, 100 mM KCI (buffer C). The column is washedwith 100 ml of buffer C, and eluted with a linear gradient of 0.0-1.0MKCl in buffer C. Fractions (7 ml each) are collected, and the presenceof apo-ACP in the fractions is detected by SDS-PAGE as described above(16% tricine gels). The fractions containing apo-ACP are pooled andapplied to an S-100 Sepharose gel filtration column (5×60 cm)equilibrated with 50 mM Tris-HCl, pH 7.0, 100 mM KCl. The column iseluted with the same buffer. Fractions (10 ml each) containing apo-ACPare collected, analyzed by electrospray mass spectrometry, and stored at−70° C. as described above.

[0220] As shown in FIG. 1, AcpS is highly expressed in E. coli, andexhibits the predicted molecular weight of approximately 13,000 daltons.The overexpressed AcpS is purified to apparent homogeneity in two stepsusing Source S-cation-exchange and gel filtration column chromatography(FIG. 1).

[0221] To confirm the purified protein as AcpS, N-terminal sequencingand mass spectrometric analyses are performed. The first 9 amino acidresidues of AcpS purified as described above are determined to beMIVGHGIDI (SEQ ID NO:6), a sequence that is identical to the predictedamino acid sequence for the protein encoded by the cloned acpS gene.This encoded protein is predicted to have a molecular weight of 13,388.Consistent with this predicted value, mass spectrometric analysis showsthat purified AcpS has a molecular weight of 13,390. Thus, the purifiedprotein is S. pneumoniae AcpS.

[0222] Analysis of AcpS by Gel Filtration Column Chromatography

[0223] To determine the native structure of AcpS, a purified AcpSpreparation (375 μg) is applied to an S-75 Superdex gel filtrationcolumn (HR 1.0×30 cm), equilibrated with 50 mM Tris-HCl, pH 7.0, 50 mMKCl, 10 mM MgCl₂. The column is calibrated with protein molecular weightstandards (Sigma). The effect of detergent or salt on the nativestructure of AcpS is analyzed by treating AcpS with 6 mM3-cholamidopropyl-dimethylammonio-1-propane sulfonate/615 (CHAPS) or50-500 mM KCl before and during column chromatography.

[0224] Sedimentation centrifugation analysis of AcpS is carried outusing an XLA 10 ultracentrifuge (Beckman Instruments, Fullerton,Calif.). A purified AcpS preparation (adjusted to 0.2 and 0.4 mg/ml) iscentrifuged at 16,000 rpm for 24 hr at 22° C. The absorbance at 280 nmas a function of radius after the system reaches equilibrium is analyzedusing XL-A/XL-1, a non-linear least squares fit data analysis program.The partial specific volume of AcpS is calculated to be 0.721 ml/g basedon its amino acid sequence. The molecular weight of AcpS is determinedusing a global fit of the two data sets collected with 0.2 and 0.4 mg/mlsamples.

[0225] Cross-linking experiments are performed as follows. Purified AcpSand apo-ACP preparations (1 ml each) are dialyzed against 2 liters of 20mM potassium phosphate buffer, pH 7.0, at 4° C. for 18 h. The dialyzedAcpS (163 μM) and apo-ACP (94 μM) preparations are mixed without or with19.5 and 9.4 mM sulfo-EGS, respectively, and the mixtures are incubatedat room temperature for 30 min. The reactions are stopped by theaddition of 50 mM Tris-base, followed by incubation at room temperaturefor 30 min.

[0226] The resulting AcpS and apo-ACP preparations treated without orwith the cross-linker (10 μl) are mixed with an equal volume of tricinesample buffer, and analyzed by SDS-PAGE (16% tricine gels).

[0227] To determine whether AcpS binds directly to apo-ACP or CoA in theabsence of the other substrate, a purified AcpS preparation (27 μM) isfirst mixed with 10 mM MgCl2, and then either 100 μM apo-ACP or 50 μMCoA. The mixture is incubated at room temperature for 30 min andsubjected to gel filtration column chromatography (S-75 Superdex) underthe conditions described above. The fractions containing theAcpS-apo-ACP complex and unbound apo-ACP are analyzed by SDS-PAGE (16%tricine gels), SYPRO Orange staining, and mass spectrometry.

[0228] Enzyme Assay And Kinetics

[0229] Unless otherwise indicated, reaction mixtures contain 50 mMTris-HCl, pH 7.0, 10 mM MgCl₂, 2.5-50 μM CoA, 0.25-6.0 μM purifiedapo-ACP of S. pneumoniae, and 3.7 nM purified AcpS of S. pneumoniae, andare incubated at 37° C. for 9 min. Reactions are stopped by the additionof 50 mM EDTA. The formation of holo-ACP is determined by an HPLC or atrichloroacetic acid (TCA) precipitation method (see below). AnHPLC-based assay is adapted from the method described previously(Lambalot and Walsh, 1997). This assay monitors the conversion ofapo-ACP to holo-ACP. Reaction mixtures (100 μl each) are injected intoan analytical HPLC column (Vydac protein C4 reverse-phase; P. J. CobertAssociates, Inc., St. Louis, Mo.) equilibrated with 45% acetonitrile in0.1% trifluoroacetic acid. The column is eluted with an 8 ml lineargradient of 45-80% acetonitrile. The column elution profiles aremonitored at 220 nm. Under these conditions, holo-ACP migrates fasterthan apo-ACP. The amount of holo-ACP formed is estimated by comparingthe peak area of the holo-ACP formed with those of both apo- andholo-ACP.

[0230] AcpS activity is also assayed by using a TCA precipitation method(Lambalot and Walsh, 1995). This method measures the incorporation ofthe 3H-labeled 4′-phospho-pantotheine group from [³H]CoA into apo-ACP.Reaction conditions are the same as those described for the HPLC assay,except that [³H]COA (specific activity, 1.5 Ci/mmol, NEN Life ScienceProducts, Boston, Mass.) is used alone or in combination with CoA.Reactions are stopped by the addition of 0.9 ml of cold 10% TCA followedby 37 μg of bovine serum albumin (BSA). Precipitated protein iscollected by centrifugation (a microfuge at 14,000 rpm) for 5 min andwashed twice with ice-cold 10% TCA. The protein collected is resuspendedin 150 μl of 1M Tris base and 0.1% Triton X-100. The resultingsuspension (100 μl) is mixed with 2.5 ml of Ready Protein+scintillationfluid (Beckman, Fullerton, Calif.), and counted using an LS 60001Cscintillation counter (Beckman).

[0231] To examine the substrate specificity of AcpS, a variety of CoAderivatives (acetyl-CoA, malonyl-CoA, acetoacetyl-CoA, desulfo-CoA, anddephospho-CoA) are tested. All reaction mixtures contain 1.5 μM apo-ACP,20 μM CoA or CoA derivative, and 19 nM AcpS, and the formation ofholo-ACP is determined by the HPLC method.

[0232] For the determination of Km and Vmax (kcat) of AcpS for apo-ACP,reaction mixtures (in quadruplicate) contain 20 μM CoA, 0.25 to 100 μMapo-ACP, and 3.7 nM. AcpS. The formation of holo-ACP is measured by theHPLC method or the TCA precipitation method. To determine Km for CoA,the reaction conditions are the same as those described above exceptthat the concentration of apo-ACP is 2.0 μM, and the concentrations ofCoA were 5 to 600 μM.

[0233] To analyze the kinetic mechanisms of AcpS, AcpS activity ismeasured at different concentrations of both substrates. Reactionmixtures (in triplicate) contain 2.5-40 μM CoA, 0.25-2.0 μM apo-ACP, and3.7 nM AcpS. The formation of holo-ACP is analyzed by the HPLC assay.

[0234] To evaluate the inhibition of AcpS activity by 3′,5′-ADP withrespect to CoA, reaction mixtures contain 1-60 μM 3′,5′-ADP, 2.5-60 μMCoA, 1.0 μM apo-ACP, and 3.7 nM AcpS. To evaluate the inhibition of AcpSactivity by 3′,5′-ADP with respect to apo-ACP, reaction mixtures contain1-60 μM 3′,5′-ADP, 0.5-6.0 μM apo-ACP, 20 μM CoA, and 3.7 nM AcpS. Theformation of holo-ACP is analyzed by the HPLC method.

[0235] Identification and Organization of the acpS and acpP Genes of S.pneumoniae

[0236] To understand the function of AcpS in the biosynthesis of fattyacids in S. pneumoniae, cloning and expression of the acpS and acpP genethat encodes a substrate of AcpS are carried out. Both genes areidentified from an S. pneumoniae data base (Baltz et al., 1998) usingthe E. coli acpS and acpP gene sequences as queries in the BLAST program(Altschul et al., 1990). The acpS gene, 369 bp long, encodes a proteinconsisting of 122 amino acid residues (SEQ ID NO: 1) with a predictedmolecular mass of 13.7 kDa (GenBank™ accession number AF276617). TheacpS gene appears to be organized into an operon with genes in the orderaroG-aroF-acpS-alr-recG as there are long non-coding regions locatedupstream of aroG and downstream of recg. Thus, the acpS operon appearsto consist of the genes that are required in aromatic amino acidbiosynthesis (aroF and aroG encoding 3-deoxy-D-arabino-heptulosonate7-phosphate synthases), cell wall biosynthesis (alr encoding D-alanineracemase), and DNA recombination (recG). In this regard, the genomicorganization of acpS in S. pneumoniae is quite different from that ofacpS in E. coli since acps in E. coli consists of an operon with itsupstream pdxj gene that is required for vitamin B6 biosynthesis (Lam etal., 1992; Takiff et al., 1992).

[0237] The acpp gene, 234 bp long, encodes a protein consisting of 77amino acid residues, with a predicted molecular weight of 8.7 kDa(GenBank™ accession number AF276618). The acpP gene appears to consistof an operon with the genes in the order hisC-unknown-plsX-acp. Thereare very long non-coding regions located in the upstream of hisC anddownstream of acpP. Like the acpS operon, the genes in the acpp operonare also involved in different aspects of cellular metabolism such ashistidine biosynthesis (his C encoding histidinol phosphateaminotransferase), lipid biosynthesis (plsx, required for the phenotypeof plsB that encodes glycerol 3-phosphate acyltransferase, an enzymerequired for lipid biosynthesis), and possibly others (unknown functiongene). It is known that the acpP genes in Bacillus subtilis, E. coli,Pseudomonas aeruginosa, and Vibrio harveyi are organized into operonswith other fatty acid biosynthetic genes (Kutchma et al., 1999;Morbidoni et al., 1996; Rawlings and Cronan, 1992; Shen and Byers,1996). Thus, the operon organization of the acpp gene in S. pneumoniaeis also different from those of the acpp genes in E. coli and otherorganisms (Kutchma et al., 1999; Morbidoni et al., 1996; Rawlings andCronan, 1992; Shen and Byers, 1996). Finally, it is known that plsx andacpp, along with other fatty acid biosynthetic genes, are also locatedin the same operon in B. subtilis, E. coli, P. aeruginosa, and V.harveyi (Kutchma et al., 1999; Morbidoni et al., 1996; Rawlings andCronan, 1992; Shen and Byers, 1996). This suggests that a geneticreorganization event might have occurred during evolution, whichresulted in the formation of the complex operons that currently exist inorganisms such as S. pneumoniae.

[0238] The subunits of S. pneumoniae AcpS and apo-ACP exhibit molecularweights virtually identical to those of E. coli AcpS and apo-ACP,respectively. Both proteins also share 38% identities with theircounterparts in E. coli. The pI value of S. pneumoniae AcpS is estimatedto be 6.5, which is much lower than 9.98, the pI value of E. coli AcpS(Lam et al., 1992; Takiff et al., 1992). Therefore, S. pneumoniae AcpSis significantly less basic than E. coli AcpS. Like other AcpS (Cronanand Rock, 1996; Rock and Cronan, 1996; Kutchma et al., 1999; Morbidoniet al., 1996; Rawlings and Cronan, 1992; Shen and Byers, 1996), S.pneumoniae apo-ACP is very acidic with a pI value of only 3.4.

[0239] Whether the S. pneumoniae acpS gene complements E. coli mutantstrain HT253, which is defective in the production of AcpS (Takiff etal., 1992), is also investigated. HT253 contains a mini-TnlO insertionin the pdxJ gene, which is upstream of and forms an operon with acpS(Lam et al., 1992; Takiff et al., 1992). The mini-Tn10 carries twodivergent tetracycline-inducible promoters (Takiff et al., 1992). In theabsence of tetracycline, HT253 cannot grow on LB plates because themini-TnlO insertion in pdxj blocks the transcription of the acpS gene.Thus, the growth of HT253 is tetracycline-dependent. When the acpS gene(pRBP123, acpS carried on pGEX-2T) is introduced into HT253, this mutantstrain is able to grow on LB medium without the supplementation oftetracycline and IPTG. Apparently, the basal level expression of acpSwithout IPTG induction is sufficient for the complementation of HT253.This result clearly shows that the S. pneumoniae acpS gene complementsthe E. coli mutant deficient in the production of AcpS. Attempts toinactivate the acpS gene of S. pneumoniae through genetic insertionalmutagenesis have failed (Baltz et al., 1997; P. Treadway, unpublishedresults), indicating that acpS is essential for growth. Since recG andair, down stream of acpS, are not essential genes (Kullik et al., 1998;Lloyd et al., 1996), we conclude that the acpS gene is essential for thegrowth of S. pneumoniae. Taken together, these results establish theidentity of the gene as acpS, and that the function of acpS is essentialfor the growth of bacterial cells.

[0240] Expression, Puirifcation, and Identification of the AcpS and ACPof S. pneumoniae

[0241] The acpS and acpP genes identified are cloned into expressionvectors and expressed in E. coli as described above. Both AcpS andapo-ACP are highly expressed in E. coli, and exhibit the molecularweights predicted (FIG. 1). The overexpressed AcpS is purified toapparent homogeneity in two steps (FIG. 1A) using SourceS-cation-exchange and gel filtration column chromatography. Theoverexpressed S. pneumoniae apo-ACP is also purified to apparenthomogeneity (FIG. 1B) in two steps using Source Q-anion exchange and gelfiltration column chromatography.

[0242] To confirm the purified proteins as AcpS and ACP, the proteinscan be subjected to N-terminal sequencing and mass spectrometricanalyses. The first 9 amino acid residues of purified AcpS aredetermined to be MIVGHGIDI (SEQ ID NO:6), a sequence that is identicalto the predicted amino acid sequence for the protein encoded by thecloned acpS gene (compare SEQ ID NO: 1). This encoded protein ispredicted to have a molecular weight of 13,388. Consistent with thispredicted value, mass spectrometric analysis shows that purified AcpShas a molecular weight of 13,390. Thus, the purified protein is S.pneumoniae AcpS.

[0243] N-terminal sequencing analysis also shows that purified apo-ACPexhibits the predicted amino acid sequence (data not shown). Whensubjected to mass spectrometric analysis, purified apo-ACP is found toexhibit two peaks. The major peak has a molecular mass of 8,834 Da(about 80% of the total protein), while the minor peak has a molecularmass of 8,861 Da (20%) that is 26 Da larger than that of the majorspecies. The predicted molecular weight for S. pneumoniae apo-ACP is8,706, in agreement with the results of mass spectrometric analysis.Mass spectrometric analysis further shows that both apo-AcpS areconverted to holo-ACP upon their reaction with AcpS, since the molecularweights of both AcpS increase by 341 Da, corresponding to the molecularweight of the 4′-phospho-pantetheine group (data not shown). Finally,mass spectrometric analysis shows that holo-ACP is not detectable in theapo-ACP preparations (data not shown).

[0244] The mobilities of apo-ACP and holo-ACP can be examined by nativegel electrophoresis followed by staining with SYPRO Orange. Holo-ACPmigrates more slowly than apo-ACP (data not shown). The completeconversion of apo-ACP to holo-ACP is confirmed by the fact that themolecular weight of ACP increases from 8,834 Da (apo-ACP) to 9,174 Da(holo-ACP) upon treatment of apo-ACP with AcpS, CoA, and Mg⁺². Thus,unlike E. coli holo-ACP (5), S. pneumoniae holo-ACP migrates more slowlythan apo-ACP.

[0245] Determination of the Native Structures of S. pneumoniae ACβS andACP

[0246] The molecular weight of native AcpS can be determined bysubjecting a purified AcpS preparation to gel filtration columnchromatography analysis. AcpS is eluted in the fractions correspondingto a molecular weight of 38 kDa (FIG. 2A, peak B). This result suggeststhat AcpS is a homotrimer with a predicted molecular mass of 41 kDa(GenBank™ accession number AF276617). To confirm this further, apurified AcpS preparation is subjected to sedimentation analysis. Thisanalysis shows that purified AcpS has a molecular mass of 39 kDa, whichis consistent with the gel filtration analysis. Finally, when a purifiedAcpS preparation is subjected to cross-linking followed by SDS-PAGEanalysis, two protein bands are observed (FIG. 3). The two bands havemolecular masses of 10.4 and 28.2 kDa, respectively, corresponding tothe monomeric and trimeric forms of AcpS (FIG. 3, lane 2). Takentogether, these results demonstrate that the AcpS of S. pneumoniae is atrimeric enzyme. The trimeric structure of AcpS appears to be stable asAcpS retains its native structure in the presence of 6 mM CHAPS or50-500 mM KCl during gel filtration column chromatography (data notshown).

[0247] When apo-ACP is subjected to gel filtration columnchromatography, it elutes in the fractions corresponding to a molecularmass of 17 kDa, indicating that apo-ACP may exist as a dimer (FIG. 2A).apo-ACP has been shown to behave abnormally on gel filtration columnsdue to its molecular asymmetry in shape (Cooper et al., 1987; Rock andCronan, 1979). To examine further whether apo-ACP is a dimer, purifiedapo-ACP is subjected to cross-linking followed by SDS-PAGE analysis.Only one protein band is observed, having a molecular mass of 5.6 kDa(FIG. 3B). This result demonstrates that apo-ACP is a monomeric protein.The result of the gel filtration column analysis is consistent with thepreviously reported anomalous behavior of apo-ACP on gel filtrationcolumns (Cooper et al., 1987; Rock and Cronan, 1979).

EXAMPLE 2 Kinetic Characterization of S. pneumoniae AcpS

[0248] To elucidate the reaction mechanism of AcpS, its substratespecificity and kinetics are examined. When assayed by the HPLC method,purified AcpS of S. pneumoniae exhibits optimal activity at 45-50° C.and pH 6.5, and is stable at 22-65° C. AcpS is able to utilize a numberof CoA derivatives as substrates, and exhibits the following relativeactivities: 100 (CoA), 91 (acetyl-CoA), 76 (desulfo-CoA), 65(acetoacetyl-CoA), 12 (malonyl-CoA), and 0 (dephospho-CoA). Thus, likeE. coli AcpS and Bacillus subtilis Sfp protein, S. pneumoniae AcpSutilizes different CoA derivatives as substrates (Gehring et al., 1997;Quadri et al., 1998).

[0249]S. pneumoniae AcpS appears to exhibit Michaelis-Menten kineticswhen assayed at various CoA concentrations and apo-ACP concentrationslower than 10 μM (FIG. 4A). AcpS activity increases in a dose-dependentmanner at apo-ACP concentrations of 0.5-5 μM (FIG. 4A). When theconcentration of apo-ACP approaches 10 μM, AcpS activity decreases (FIG.4A). This result is consistent with the observation that apo-ACP isinhibitory to AcpS at higher concentrations (Elovson and Vagelos, 1968;Lambalot and Walsh, 1995; Flugel et al., 2000; Gehring et al., 1997).However, a further increase of apo-ACP concentrations (>10 μM) isaccompanied by a significant increase in AcpS activity (FIG. 4A). As aresult, two separate substrate saturation curves are obtained at low andhigh concentrations of apo-ACP (FIG. 4, B and C). Double reciprocal plotanalyses indicate that AcpS has Km (for apo-ACP) values of 0.5±0.08 and109±6.8 μM, and Vmax values of 2439±243 (kcat=1.7±0.17 s-1) and13659±1290 (kcat=9.3±0.9 s-1) nmol/min/mg at the low and highconcentrations of apo-ACP, respectively. Thus, at higher apo-ACPconcentrations, the affinity of AcpS for apo-ACP is significantlydecreased (approximately 200-fold), but its catalytic activity issignificantly increased (5-fold). Together, these results indicate thatthe S. pneumoniae AcpS may be allosterically regulated by its substrate,apo-ACP.

[0250] When a fixed apo-ACP concentration and various CoA concentrationsare used, a hyperbolic substrate saturation curve is obtained for AcpS(FIG. 5A). The apparent Km and Vmax values of AcpS are determined to be11.5±0.9 μM (for CoA) and 3976±73 nmol/min/mg (kcat=2.7±0.05 s-1),respectively (FIG. 5B). The kcat values determined for AcpS at lowapo-ACP concentrations are thus in good agreement (1.7 versus 2.7 s⁻¹).

[0251] Since the TCA precipitation method has been often used for theassay of AcpS activity (Elovson and Vagelos, 1968; Lambalot and Walsh,1995; Flugel et al., 2000), we also characterize the kinetic propertiesof the enzyme using this assay method. This assay utilizes [³H]CoA as asubstrate for AcpS. The apparent Km values of the enzyme for apo-ACP andCoA are determined to be 1.3±0.7 and 7.1±0.4 μM, respectively. The Vmax(kcat) values determined are 4179±182 (2.8±0.04 s⁻¹) nmol/min/mg. Thus,the kinetic parameters determined by the TCA precipitation method are ingeneral agreement with those obtained by the UPLC method. However, wedid notice that the TCA precipitation method tends to generatevariations significantly higher than those of the HPLC method,especially when apo-ACP is below 1 μM.

[0252] Although E. coli AcpS has been extensively studied (Elovson andVagelos, 1968; Lambalot and Walsh, 1995; Flugel et al., 2000; Lambalotet al., 1996), the kinetic mechanism of this enzyme is unknown. Toelucidate further the kinetic mechanism of S. pneumoniae AcpS, doublereciprocal plots of the initial velocities of the enzyme at fixedconcentrations of one substrate versus various concentrations of theother substrate (Copeland, 1996) are analyzed. This analysis yields Kmand Vmax values that are similar to those determined before (data notshown). As shown in FIG. 6A, the double reciprocal plots of the initialvelocities of AcpS obtained at the various CoA and fixed apo-ACPconcentrations yields an intersecting pattern. The same pattern isobtained when various concentrations of apo-ACP and fixed concentrationsof CoA are used (FIG. 6B). Taken together, these results suggest thatAcpS proceeds by a random or compulsory ordered bi bi type, but not aping-pong (double displacement) type, of reaction mechanism (Copeland,1996).

[0253] To differentiate these two possible reaction mechanisms, thekinetics of product inhibition are analyzed. AcpS activity is examinedin the presence of 3′,5′-ADP. As shown in FIG. 7A, when various CoAconcentrations are used, the double reciprocal plots yield a simplecompetitive pattern with a Ki of 6.0 μM (FIG. 7C). However, when variousapo-ACP concentrations are used, the double reciprocal plots yield alinear-mixed pattern with a Ki of 2.5 μM (FIG. 7, A and D). Since thepatterns of inhibition with respect to CoA and apo-ACP are competitiveand mixed, respectively, these results suggest that apo-ACP is probablythe first substrate to bind to the enzyme, which is followed by CoA(Copeland, 1996).

EXAMPLE 3 Binding of apo-ACP and CoA to AcpS

[0254] The order of substrate binding to AcpS can be analyzed bydetermining the binding of CoA and apo-ACP to purified AcpS by gelfiltration column chromatography, mass spectrometry, or filter bindingassays. If CoA binds to AcpS first and forms an enzyme-substrate complexthat is required for the next reaction with apo-ACP, then a stableenzyme-substrate complex should be detectable. When a mixture of CoA andpurified AcpS incubated at room temperature for 30 min is subjected togel filtration column chromatographic and mass spectrometric analyses,the CoA is not detectable in the fractions containing purified AcpS(data not shown). Thus, CoA does not appear to bind to AcpS in theabsence of apo-ACP. To examine further the binding of CoA to AcpS, amixture of purified AcpS and [³H]CoA incubated under the same conditionsis subjected to a filter binding assay. Under these conditions, [³H]CoAdoes not appear to bind to AcpS as the radioactivity of [3H]CoA is notdetectable after washing (data not shown). Consistent with the foregoingevidence, CoA does not appear to bind to AcpS in the absence of apo-ACP.

[0255] Whether apo-ACP binds to AcpS in the absence of CoA, a mixture ofAcpS and apo-ACP (apo-ACP/AcpS=5:1) can be subjected to gel filtrationcolumn chromatography and analysis of the column fractions by SDS-PAGE.Two protein peaks are observed (FIG. 2A). The leading peak (peak A) hasa molecular mass of approximately 53 kDa as judged by gel filtrationanalysis (FIG. 2A). Since AcpS exists as a trimer with a molecular massof approximately 41 kDa, this leading peak probably represents a complexbetween apo-ACP and AcpS (FIG. 2A). Consistent with the formation of theAcpS-apo-ACP complex, the presence of apo-ACP is also detected in thefractions containing purified AcpS (FIG. 2B). Together, these resultsdemonstrate that apo-ACP can bind to AcpS in the absence of CoA. Insummary, the analysis of the initial velocities of AcpS obtained atfixed concentrations of one substrate and various concentrations ofanother reveals that catalysis by AcpS probably proceeds by a random orordered compulsory bi bi reaction mechanism because an intersectingpattern was obtained regardless of which substrate (CoA or apo-ACP) wasthe fixed one or the varied one (Copeland, 1996) (FIG. 6). Theinhibition kinetics of 3′,5′-ADP, one of the reaction products,indicates that AcpS catalysis appears to proceed by an ordered reactionmechanism, with the initial formation of an AcpS-apo-ACP intermediateand the subsequent transfer of 4′-phosphopantetheine from CoA ontoapo-ACP. The mode of inhibition by 3′,5′-ADP with respect to CoA iscompetitive when apo-ACP is the fixed substrate and CoA is the variedsubstrate (FIG. 7). The competitive inhibition with respect to CoAindicates that CoA only binds to the enzyme-apo-ACP intermediate. Themode of inhibition by 3′,5′-ADP with respect to apo-ACP is mixed, i.e.,a combination of competitive and noncompetitive inhibition when apo-ACPis the varied substrate and CoA is the fixed substrate (FIG. 7B). Themixed type of inhibition by 3′,5′-ADP with respect to apo-ACP suggeststhat 3′,5′-ADP binds to the free enzyme and the enzyme-apo-ACPintermediate. Thus, inhibition is competitive with respect to apo-ACPwhen 3′,5′-ADP binds to the free enzyme, and noncompetitive with respectto apo-ACP when 3′,5′-ADP binds to the enzyme-apo-ACP intermediate. Thisproposed reaction mechanism for AcpS is consistent with the results ofthe substrate-binding experiments. Under the conditions tested, apo-ACPbinds tightly to AcpS in the absence of CoA, but CoA fails to bind inthe absence of apo-ACP. Taken together, these results suggest that thereaction mechanism of AcpS is ordered rather than random, and that theformation of the enzyme-apo-ACP intermediate occurs prior to thetransfer of 4′-phosphopantethine from CoA onto apo-ACP.

EXAMPLE 4 Crystallization of AcpS; Data Collection, Structure Solution,and Refinement

[0256] Production and Purification of Selenomethionine-Containing AcpS

[0257] Selenomethionine is incorporated into AcpS using the method ofDoublie, 1997, which is based on inhibition of the methioninebiosynthetic pathway. One ml of E. coli BL21 (pLysS) cells containingpETI la that carries the acpS gene of S. pneumoniae from an overnightculture in LB medium is centrifuged, and resuspended in 1 ml of M9minimal medium (Sambrook et al., 1989) supplemented with 100 μg/mlampicillin and 4 g/L glucose. This 1 ml suspension is added to 1 literof the same medium pre-warmed at 33° C. Cells are grown at 33° C. withshaking at 250 rpm to an optical density of 0.5-0.6 at 590 nm (mid-logphase) before addition of amino acids as follows: lysine, phenylalanine,and threonine at 100 mg/L; isoleucine, leucine, and valine at 50 mg/L;and L-selenomethionine at 60 mg/L. Expression is induced with 1 mM IPTG15 min after adding amino acids, and continued for 18 hours. The cellsare harvested, and AcpS is purified as described above, the onlymodifications being the addition of 1 mM dithiothreitol (DTT) to thepurification buffers to prevent oxidation of the seleno-methioninegroups, and Mono Q chromatography.

[0258] The fractions from the gel filtration FPLC step containing AcpS(verified by 16% Tricine SDS-PAGE) are pooled and applied directly to aMono Q ion exchange FPLC column (1 ml bed volume) (Pharmacia)equilibrated in 50 mM Tris-HCl, pH 7.0. The column is washed for 10 bedvolumes (10 mls) in this buffer, and then a 0M to 1M KCl gradient isapplied. The column is run at 1.0 ml/min, detection is at 280 nm, and 1ml fractions are collected. The fractions are analyzed by 16% tricineSDS-PAGE. Fractions containing AcpS are pooled, dialyzed against 50 mMTris-HCl, pH 7.0, 140 mM KCl, 10 mM MgCl₂, analyzed for proteinconcentration using Bradford Protein assay (BioRad Laboratories) andbovine serum albumin as a standard. The resulting protein solution isthen used for crystallography.

[0259] Crystallization of AcpS

[0260] Diffraction-quality crystals are grown by the vapor diffusiontechnique at 294K. The protein is concentrated using a Centricon filter(molecular weight cutoff=10 kDa) to 8 mg/ml in a solution of 10 mMMgCl₂, 14 mM KCl, and 20 mM Tris-HCl buffer at pH 7.1. A 4 μl (1:1, v/v,protein/reservoir solution) drop is equilibrated in a 500 μl solutioncontaining 8-15% PEG 4000, 200 mM ammonium sulfate, and 100 mM citratebuffer at pH 4.5. Crystals of AcpS are obtained after 4 to 5 days atroom temperature. Crystals belong to orthorhombic space group P2₁2₁2₁(unit cell parameters a=49.8 Å, b=59.6 Å, c=114.7 Å) (Native 1; Tables 2and 3). Crystallization conditions similar to those described above alsoyield crystals that belong to monoclinic space group C2 (unit cellparameters a=120.2 Å, b=62.3 Å, c=51.7 Å, β=98.7°) for apo-AcpS (Native2; Tables 2 and 4) and 3′,5′-ADP complex (Tables 2 and 5). Both crystalforms have a homotrimeric molecule per asymmetric unit, with a Vm value(Matthews, 1968) of 2.08 Å³/Da, which corresponds to a solvent contentof approximately 41% in both cases. CoA, in 2-3 fold of excess of theprotein, is used as a starting material for co-crystallization in the3′,5′-ADP complex.

[0261] Data Collection, Structure Solution, and Refinement

[0262] The diffraction data are collected using a MarCCD detector onIMCA (Industrial Macromolecular Crystallography Association) beam lineID-17 at the APS (Advanced Photon Source, Argonne National Laboratories)at 100K, using 15-20% glycerol as a cryoprotectant. The diffraction dataare reduced using DENZO (HKL2000) (Otwinowski and Minor 1997), and theintensities are scaled with SCALEPACK (Collaborative Computing Project,No. 4, 1994). Most calculations are performed with the CCP4 suite ofprograms (Collaborative Computing Project, No. 4, 1994). Multipleanomalous dispersion (MAD) data at three wavelengths around the seleniumK-shell edge are collected from a single crystal(selenomethionine-substituted protein) belonging to the P2₁2₁2₁ spacegroup at 2.8 Å resolution using the inverse beam strategy (Hendricksonet al., 1991). Location of the Se sites and phasing are performed usingSOLVE (Terwilliger and Berendzen, 1999), resulting in a figure of meritof 0.64 for the data in the resolution range 20-2.8 Å. Experimentalphases are subsequently modified by the application of solventflattening and 3-fold NCS averaging using the program DM (CollaborativeComputing Project, No. 4, 1994). The experimental map allows tracing of115 amino acid residues, excluding the three-residue loop correspondingto residues Gly69-Lys73, and the four C-terminal residues for eachmonomer molecule of the homotrimer. This model is refined against databetween 20 and 2.4 Å using a maximum likelihood algorithm asincorporated in the program CNX2000 (Badger et al., 1999)(R_(work)=0.236, R_(free)=0.293) (Brünger, 1992). Subsequently, thecoordinates of the trimer are used as a search model in molecularreplacement (AmoRe) (Navaza, 1994) for the C2 space group crystals. Thisstructure is refined to an R_(work) of 0.208 (R_(free)=0.247) againstthe data in the resolution range of 20-2.0 Å. The AcpS/3′,5′-ADP complexstructure is refined to an R_(work) of 24.1% (R_(free)=27.1%) for the20-1.9 Å resolution range. The program suite QUANTA 98 (MolecularSimulation Inc., San Diego, Calif.) is used for visual inspection andmanual corrections between rounds of refinement. An analysis of thegeometry shows that all parameters are within the values expected for amodel at this resolution. All residues are found in the most favorableand additionally allowed regions of a Ramachandran plot for all threecrystal structures. The last four residues in each AcpS protomer andresidues Gly69-Lys7l of a disordered surface loop for one of thesubunits are not defined in the electron density even aftercrystallographic refinement, and for this reason are not included in thefinal model. The overall average temperature factor of the structuresare in good agreement with that calculated from the Wilson plot.

[0263] Coordinates are deposited in the PDB under entry codes 1FTE,1FTF, and 1FTH.

EXAMPLE 5 Overall Structure of Apo-AcpS

[0264] Data are collected from crystals and the structure of AcpS solvedby the multiple anomalous dispersion method (MAD) (Hendrickson et al.,1991) using selenomethionine-substituted protein and exploitingnon-crystallographic 3-fold averaging. The atomic coordinates of nativeAcpS (Native 1 and Native 2) are shown in Tables 3 and 4, respectively.The crystallographic data collection statistics and refinementparameters are summarized in Table 2.

[0265] The structure of AcpS reveals that it assembles as a tightlypacked homotrimer. The overall view of the AcpS molecule is shown inFIG. 8A. The AcpS monomer has an elongated elliptical shape withapproximate dimensions of 30×35×45 Å (FIG. 8B). The Richardson topologydiagram of secondary structural elements is shown in FIG. 8C. Thelocation of these secondary structure elements within the proteinsequence is given in Table lA. The AcpS structure has an α/β fold. Atopology search using the SCOP program (Murzin et al 1995) does notreveal any significant similarity with AcpS. The AcpS protomer ischaracterized primarily by three structural motifs. The first is aclassical three-stranded anti-parallel β-sheet formed by strands β1, β5,and β4. A long α-helix packs diagonally against the β-sheet togetherwith α-helixes α1, α2, α3, and α4 of the anti-parallel four helicalbundle, which represents the second structural motif. The third featureconsists of a long extended loop with a two-strand anti-parallel β-sheetβ2 and β3). These structural motifs are organized in such a way that thelong helix α4 runs through the whole structure and is surrounded by theother structural elements.

[0266] The side chains of each helix in the four-helical bundle arearranged so that hydrophobic side chains are buried between the helicesand form a hydrophobic core comprised of Ile 17, Ala 20, Val 21 (α1);Phe 27, Ala 28, Val 31, Leu 32 (α2); Met 37, Phe 40 (α3); Ile 49, Leu52, Trp 56 (α4). Side chains of the residues Phe 75 and Ile 70 (α5) alsoparticipate in the formation of this hydrophobic cluster. Anotherhydrophobic cluster is formed by the long α-helix α4, and the three- andtwo-stranded β-sheets, which contain side chains of the residues Phe 62,Met 66 (α4); Phe 90 (β3); Phe 95, Ile99 (β4).

[0267] The final refined structure of AcpS contains 115 out of 122 aminoacids. No electron density is observed for the first two N-terminal andfinal four C-terminal amino acids. The three protomers are related by anon-crystallographic 3-fold pseudo symmetry axis. The three-strandedanti-parallel β-sheets of each AcpS protomer are arranged together in abarrel-like structure in the homotrimer molecule, forming a long, mostlyhydrophobic tunnel that runs through the whole structure. The activesites are formed at the intermolecular interface of the homotrimer (FIG.8B) such that two protomers contribute to the formation of each activesite. An active site pocket is formed by residues of helix α4, 1-strandsβ4 and β5, and loop β2-β3 of one protomer, and the opposite side ofhelix α4, β-stranded β5 and loop α4-α5 of the second protomer molecule.Since the AcpS active site is created by the interface between twomonomers, which are oriented by their homotrimer architecture, thetrimeric structure of AcpS appears to be essential for activity. This isconsistent with the results of dynamic light scattering (ProteinSolution Inc., Charlottesville, Va.), gel filtration columnchromatography, and sedimentation analysis of the purified AcpS, whichdemonstrate that AcpS is a homotrimer (note Example 1 and McAllister etal., 2000). Finally, the native structure reveals that only two out ofthree active sites are occupied by sulfate ions that are present duringthe crystallization of AcpS. The sulfate ions are found to be present inthe vicinity of His105, Asp10, and Lys64, which corresponds to theα-phosphate of CoA (see below).

EXAMPLE 5 Co-Crystallization of Purified AcpS with Coenzyme A; OverallStructure of the AcpS/3′,5′-ADP Complex

[0268] To help identify the potential active site of AcpS for astructure-based design effort, purified AcpS is co-crystallized withCoA, a substrate of AcpS. Surprisingly, however, the purified AcpS isco-crystallized with 3′,5′-ADP, a product of the AcpS reaction. The factthat only the 3′,5′-ADP moiety exhibits a well defined electron densityclearly demonstrates that 3′,5′-ADP, rather than CoA, co-crystallizeswith AcpS. Consistent with the native structure of AcpS, the structureof the AcpS/3′,5′-ADP complex shows that AcpS is a trimeric enzyme. Inaddition, only two out of three active sites are occupied by 3′,5′-ADPin this case, rather than sulfate ions as in the case of the nativestructure, thus indicating that the binding of the 3′,5′-ADP moleculesto AcpS competes with that of the sulfate ions. These results are alsoin good agreement with those of gel filtration and SDS-PAGE analysis(supra, and McAllister et al., 2000) which demonstrate that ACP is boundto AcpS in a 2:3 ratio. Finally, similar to that of the nativestructure, the unoccupied active site of the complex structure alsoexhibits no defined electron density for residues Ile70-Leu73 of theα4-α5 loop. Thus, the complex structure of AcpS suggests that the activeform of the enzyme is trimeric.

[0269] The atomic coordinates of the AcpS/3′,5′-ADP complex are shown inTable 5; the active site of the AcpS/3′,5′-ADP complex is shown in FIG.9. The 3′,5′-ADP binding site is characterized by the followingstructural elements. The adenine base fits in between loop β2-β3 (Gly86,Ala87, and Pro88) and loop α4-α5 (Lys64, Gly67, and Thr68) from anotherprotomer of the AcpS trimer. An amino group of the adenine ring is in afavorable position to form a hydrogen bond with a carbonyl oxygen ofArg85 and Thr68. The ribose moiety is bound to the adenine ring with ananti-glycosidic torsion angle. The ribose is present in a 3′-endoconformation with the axial orientation of the 2′-hydroxyl and theequatorial orientation of the 3′-phosphate group. The 3′-phosphateportion of the ligand has an interaction with loop β2-β3, α4, and β4,all of which belong to the first protomer. The 3′-phosphate issurrounded by a negatively charged cluster formed by Arg39, Arg47, andArg55. The 5′ α-phosphate is packed against β1 and α4 of the secondprotomer, and has hydrogen bonds with Lys64, Ser104, and His105.

[0270] In summary, AcpS, which catalyzes the transfer of4′-phosphopantetheine from CoA to apo-ACP to form holo-ACP along withthe production of 3′,5′-ADP, is an attractive target for the developmentof antibacterial drugs. The structure of AcpS reveals an α/β fold, anddemonstrates that the trimeric structure of the enzyme appears to beessential for the AcpS activity. These results represent the firststructural determination of the interaction between the AcpS enzyme andits product, 3′,5′-ADP. These data provide a starting point forstructure-based diagnostics, and drug design efforts that will enableidentification of novel AcpS inhibitors with potent antibacterialactivity useful in treating bacterial infections.

[0271] The invention being thus described, it is obvious that the samecan be varied in many ways. Such variations are not to be regarded as adeparture from the spirit and scope of the present invention, and allsuch modifications as would be obvious to one skilled in the art areintended to be included within the scope of the following claims.

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[0359] TABLE 1B

[0360] TABLE 2 Crystallographic data Inflection, L1 Peak, L2 Remote, L3Native 1 ^(&)Native 2 ^(&)3′5′-ADP Data collection Energy, eV 12,655.7512,659.28 12,700.00 12,398.00 12,398.00 12,398.00 Wavelength λ, Å0.979537 0.979400 0.976259 1.00000 1.00000 1.00000 Number ofobservations 210,097 205,948 211,823 336,325 423,425 304,946 Number ofreflections 54,462 55,080 54,821 59,335 126,451 162,841 Number of uniquereflections 8,450 8,508 8,398 14,842 20,366 29,541 Average redundancy6.4 6.5 6.5 4.0 6.2 5.5 Completeness, % All reflections ^(a)95/90  95/8894/88 96/84 94/89 100/99  Reflections with I > 3σ 94/85 94/86 94/8481/57 79/53 80/44 <I/σ> overall 40/14 41/19 40/18 25.6/4.5  26.5/3.0 31.1/3.8  *R_(merge), % 5.6/9.2 5.2/8.8 4.7/8.4  4.9/23.0  6.0/30.1 5.3/26.8 Resolution, Å 2.8 2.8 2.8 2.4 2.0 1.9 Refinement Protein/Water2,696/128   2,730/125   2,717/177   Deviation form ideal geometry bondlength, Å/bond angles, ° 0.007/1.169 0.005/1.057 0.010/1.146dihedrals/imprpers, ° 25.956/0.588  23.123/0.610  22.247/0.770 Ramachandran plot statistics Residues in most favorite/allowed regions,% 92.0/8.0  91.2/9.0  92.4/7.6  †R_(work)/^(¶)R_(free), % 23.6/29.320.8/24.7 24.1/27.1

[0361] TABLE 3 REMARK coordinates from restrained individual B-factorrefinement REMARK refinement resolution: 500.0-2.40 A REMARK starting r= 0.2339 free_r = 0.2899 REMARK final r = 0.2336 free_r = 0.2950 REMARKB rmsd for bonded mainchain atoms = 0.775 target = 1.5 REMARK B rmsd forbonded sidechain atoms = 0.798 target = 2.0 REMARK B rmsd for anglemainchain atoms = 1.417 target = 2.0 REMARK B rmsd for angle sidechainatoms = 1.333 target = 2.5 REMARK wa = 3.19192 REMARK rweight = 0.44902REMARK target = mlf   steps = 30 REMARK sg = P2(1)2(1)2(l) a = 49.824 b= 59.561 c = 113.738 alpha = 90 beta = 90 gamma = 90 REMARK parameterfile 1: CNX_TOPPAR:protein_rep.param REMARK parameter file 2:CNX_TOPPAR:water_rep.param REMARK parameter file 3: CNX_TOPPAR:ion.paramREMARK parameter file 4: so4/so4.param REMARK molecular structure file:generate.psf REMARK input coordinates: minimize.pdb REMARK reflectionfile = x-ray_data.cv REMARK ncs = none REMARK B-correction resolution:6.0-2.40 REMARK initial B-factor correction applied to fobs: REMARK  B11= 5.613  B22 = 4.955  B33 = −10.569 REMARK  B12 = 0.000  B13 = 0.000 B23 =   0.000 REMARK B-factor correction applied to coordinate arrayB:  0.171 REMARK bulk solvent: (Mask) density level = 0.356315e/A{circumflex over ( )}3, B-factor = 44.7059 A{circumflex over ( )}2REMARK reflections with |Fobs|/sigma_F < 0.0 rejected REMARK reflectionswith |Fobs| > 10000 * rms(Fobs) rejected REMARK theoretical total numberof refl. in resol. range: 13818 (100.0%) REMARK number of unobservedreflections (no entry or |F| = 0): 537 ( 3.9%) REMARK number ofreflections rejected: 0 ( 0.0%) REMARK total number of reflections used:13281 ( 96.1%) REMARK number of reflections in working set: 12603( 91.2%) REMARK number of reflections in test set: 678 ( 4.9%) REMARKFILENAME = “acps_native 1.pdb” REMARK Written by CNX VERSION: 2000 ATOM1 CB MET A1003 6.910 33.184 39.062 1.00 31.51 C ATOM 2 CG MET A10035.553 33.663 38.598 1.00 33.32 C ATOM 3 SD MET A1003 4.818 34.801 39.8161.00 36.27 S ATOM 4 CE MET A1003 5.820 36.290 39.557 1.00 35.34 C ATOM 5C MET A1003 7.655 32.931 36.686 1.00 29.56 C ATOM 6 O MET A1003 8.28633.972 36.449 1.00 29.16 O ATOM 7 N MET A1003 9.076 32.131 38.552 1.0030.78 N ATOM 8 CA MET A1003 7.675 32.305 38.074 1.00 30.32 C ATOM 9 NILE A1004 6.935 22.292 35.768 1.00 28.43 N ATOM 10 CA ILE A1004 6.82632.791 34.401 1.00 27.65 C ATOM 11 CB ILE A1004 6.307 31.701 33.452 1.0028.01 C ATOM 12 CG2 ILE A1004 6.103 32.287 32.051 1.00 27.49 C ATOM 13CG1 ILE A1004 7.294 30.525 33.430 1.00 27.59 C ATOM 14 CD1 ILE A10046.890 29.404 32.482 1.00 28.22 C ATOM 15 C ILE A1004 5.885 33.992 34.3221.00 26.94 C ATOM 16 O ILE A1004 4.741 33.920 34.765 1.00 26.43 O ATOM17 N VAL A1005 6.380 35.088 33.750 1.00 25.94 N ATOM 18 CA VAL A10055.595 36.306 33.617 1.00 25.33 C ATOM 19 CB VAL A1005 6.211 37.44634.445 1.00 25.03 C ATOM 20 CG1 VAL A1005 6.389 36.995 35.882 1.00 25.00C ATOM 21 CG2 VAL A1005 7.535 37.878 33.846 1.00 24.19 C ATOM 22 C VALA1005 5.432 36.796 32.173 1.00 25.45 C ATOM 23 O VAL A1005 4.982 37.92031.949 1.00 25.63 O ATOM 24 N GLY A1006 5.794 35.964 31.197 1.00 25.11 NATOM 25 CA GLY A1006 5.659 36.371 29.809 1.00 24.32 C ATOM 26 C GLYA1006 6.306 35.452 28.786 1.00 23.99 C ATOM 27 O GLY A1006 7.413 34.94728.996 1.00 24.03 O ATOM 28 N HIS A1007 5.613 35.232 27.671 1.00 23.11 NATOM 29 CA HIS A1007 6.132 34.386 26.603 1.00 22.22 C ATOM 30 CB HISA1007 5.633 32.943 26.789 1.00 22.37 C ATOM 31 CG HIS A1007 6.046 32.01025.693 1.00 22.55 C ATOM 32 CD2 HIS A1007 5.331 31.123 24.961 1.00 22.89C ATOM 33 ND1 HIS A1007 7.342 31.933 25.226 1.00 22.71 N ATOM 34 CE1 HISA1007 7.405 31.044 24.251 1.00 22.72 C ATOM 35 NE2 HIS A1007 6.19830.537 24.070 1.00 22.98 N ATOM 36 C HIS A1007 5.718 34.925 25.234 1.0021.79 C ATOM 37 O HIS A1007 4.553 35.230 25.007 1.00 21.69 O ATOM 38 NGLY A1005 6.682 35.054 24.325 1.00 21.62 N ATOM 39 CA GLY A1008 6.38035.549 22.994 1.00 20.43 C ATOM 40 C GLY A1005 7.237 34.888 21.932 1.0020.87 C ATOM 41 O GLY A1008 8.396 34.554 22.171 1.00 20.58 O ATOM 42 NILE A1009 6.655 34.663 20.760 1.00 20.92 N ATOM 43 CA ILE A1009 7.38934.077 19.652 1.00 21.06 C ATOM 44 CB ILE A1009 6.911 32.638 19.304 1.0021.27 C ATOM 45 CG2 ILE A1009 7.140 31.699 20.485 1.00 21.48 C ATOM 46CG1 ILE A1009 5.438 32.654 18.892 1.00 21.01 C ATOM 47 CD1 ILE A10094.967 31.340 18.285 1.00 20.98 C ATOM 48 C ILE A1009 7.184 34.951 18.4201.00 21.74 C ATOM 49 O ILE A1009 6.345 35.846 18.404 1.00 20.69 O ATOM50 N ASP A1010 7.971 34.687 17.388 1.00 22.85 N ATOM 51 CA ASP A10107.857 35.416 16.147 1.00 23.91 C ATOM 52 CB ASP A1010 8.456 36.81316.273 1.00 23.93 C ATOM 53 CG ASP A1010 8.300 37.622 14.998 1.00 24.40C ATOM 54 OD1 ASP A1010 9.104 37.423 14.050 1.00 24.86 O ATOM 55 OD2 ASPA1010 7.357 38.442 14.939 1.00 24.36 O ATOM 56 C ASP A1010 8.553 34.65815.041 1.00 24.83 C ATOM 57 O ASP A1010 9.586 34.037 15.262 1.00 25.16 OATOM 58 N ILE A1011 7.959 34.687 13.852 1.00 25.82 N ATOM 59 CA ILEA1011 8.541 34.021 12.697 1.00 27.04 C ATOM 60 CB ILE A1011 7.713 32.78012.258 1.00 26.91 C ATOM 61 CG2 ILE A1011 6.274 33.168 11.940 1.00 26.65C ATOM 62 CG1 ILE A1011 8.378 32.126 11.048 1.00 27.05 C ATOM 63 CD1 ILEA1011 7.818 30.757 10.708 1.00 27.44 C ATOM 64 C ILE A1011 8.586 35.05111.580 1.00 27.96 C ATOM 65 O ILE A1011 7.652 35.832 11.404 1.00 28.18 OATOM 66 N GLU A1012 9.688 35.070 10.845 1.00 28.86 N ATOM 67 CA GLUA1012 9.841 36.023 9.762 1.00 30.03 C ATOM 68 CB GLU A1012 10.772 37.16110.186 1.00 31.54 C ATOM 69 CG GLU A1012 10.071 38.292 10.895 1.00 33.83C ATOM 70 CD GLU A1012 9.006 38.913 10.026 1.00 35.22 C ATOM 71 OE1 GLUA1012 9.352 39.404 8.927 1.00 36.13 O ATOM 72 OE2 GLU A1012 7.825 38.90310.438 1.00 36.10 O ATOM 73 C GLU A1012 10.375 35.414 8.487 1.00 29.94 CATOM 74 O GLU A1012 11.219 34.526 8.513 1.00 29.44 O ATOM 75 N GLU A10139.864 35.901 7.367 1.00 30.50 N ATOM 76 CA GLU A1013 10.331 35.444 6.0691.00 30.96 C ATOM 77 CE GLU A1013 9.236 35.587 5.012 1.00 31.74 C ATOM78 CG GLD A1013 9.629 34.951 3.693 1.00 33.86 C ATOM 79 CD GLU A10138.621 35.179 2.582 1.00 35.01 C ATOM 80 OE1 GLU A1013 8.792 34.550 1.5151.00 36.28 O ATOM 81 OE2 GLU A1013 7.675 35.980 2.762 1.00 35.21 O ATOM82 C GLU A1013 11.498 36.372 5.735 1.00 30.42 C ATOM 83 O GLU A101311.348 37.594 5.750 1.00 30.06 O ATOM 84 N LEU A1014 12.662 35.800 5.4571.00 30.14 N ATOM 85 CA LEU A1014 13.824 36.617 5.140 1.00 30.32 C ATOM86 CB LEU A1014 15.022 35.722 4.814 1.00 30.23 C ATOM 87 CG LEU A101415.552 34.904 6.000 1.00 30.34 C ATOM 88 CD1 LEU A1014 16.618 33.9295.533 1.00 30.59 C ATOM 89 CD2 LEU A1014 16.117 35.835 7.053 1.00 30.41C ATOM 90 C LEU A1014 13.526 37.563 3.977 1.00 30.65 C ATOM 91 O LEUA1014 13.877 38.743 4.023 1.00 30.37 O ATOM 92 N ALA A1015 12.857 37.0482.949 1.00 30.96 N ATOM 93 CA ALA A1015 12.519 37.855 1.784 1.00 31.57 CATOM 94 CB ALA A1015 11.683 37.038 0.798 1.00 30.98 C ATOM 95 C ALAA1015 11.780 39.131 2.183 1.00 31.93 C ATOM 96 O ALA A1015 11.947 40.1701.544 1.00 31.75 O ATOM 97 N SER A1016 10.972 39.055 3.240 1.00 32.40 NATOM 98 CA SER A1016 10.227 40.224 3.714 1.00 33.29 C ATOM 99 CB SERA1016 9.264 39.844 4.847 1.00 33.61 C ATOM 100 OG SER A1016 8.316 38.8834.428 1.00 34.88 O ATOM 101 C SER A1016 11.194 41.279 4.235 1.00 33.73 CATOM 102 O SER A1016 11.059 42.464 3.937 1.00 33.37 O ATOM 103 N ILEA1017 12.156 40.828 5.035 1.00 34.48 N ATOM 104 CA ILE A1017 13.16741.698 5.615 1.00 35.17 C ATOM 105 CB ILE A1017 14.041 40.922 6.641 1.0034.97 C ATOM 106 CG2 ILE A1017 15.151 41.814 7.173 1.00 34.62 C ATOM 107CG1 ILE A1017 13.172 40.436 7.805 1.00 35.03 C ATOM 108 CD1 ILE A101712.550 41.555 8.623 1.00 34.83 C ATOM 109 C ILE A1017 14.064 42.2664.516 1.00 35.70 C ATOM 110 O ILE A1017 14.435 43.439 4.555 1.00 35.49 OATOM 111 N GLU A1018 14.414 41.431 3.542 1.00 36.59 N ATOM 112 CA GLUA1018 15.260 41.872 2.439 1.00 38.02 C ATOM 113 CB GLU A1018 15.59540.703 1.508 1.00 39.36 C ATOM 114 CG GLU A1018 16.768 40.993 0.578 1.0042.30 C ATOM 115 CD GLU A1018 16.928 39.967 −0.532 1.00 44.15 C ATOM 116OE1 GLU A1018 16.923 38.748 −0.239 1.00 45.23 O ATOM 117 OE2 GLU A101817.069 40.387 −1.703 1.00 45.34 O ATOM 118 C GLU A1018 14.480 42.9251.658 1.00 38.06 C ATOM 119 O GLU A1018 15.026 43.936 1.212 1.00 37.81 OATOM 120 N SER A1019 13.187 42.668 1.509 1.00 37.94 N ATOM 121 CA SERA1019 12.297 43.561 0.799 1.00 37.74 C ATOM 122 CB SER A1019 10.92142.906 0.680 1.00 37.89 C ATOM 123 OG SER A1019 9.994 43.764 0.044 1.0038.96 O ATOM 124 C SER A1019 12.182 44.916 1.505 1.00 37.72 C ATOM 125 OSER A1019 12.074 45.957 0.850 1.00 37.89 O ATOM 126 N ALA A1020 12.20744.902 2.836 1.00 37.14 N ATOM 127 CA ALA A1020 12.097 46.129 3.615 1.0037.01 C ATOM 128 CB ALA A1020 11.773 45.800 5.063 1.00 36.69 C ATOM 129C ALA A1020 13.369 46.973 3.542 1.00 37.03 C ATOM 130 O ALA A1020 13.30948.201 3.538 1.00 36.27 O ATOM 131 N VAL A1021 14.519 46.309 3.497 1.0037.47 N ATOM 132 CA VAL A1021 15.797 47.007 3.415 1.00 38.34 C ATOM 133CB VAL A1021 16.979 46.047 3.651 1.00 37.99 C ATOM 134 CG1 VAL A102118.282 46.740 3.316 1.00 38.47 C ATOM 135 CG2 VAL A1021 16.990 45.5855.093 1.00 38.14 C ATOM 136 C VAL A1021 15.937 47.605 2.025 1.00 38.86 CATOM 137 O VAL A1021 16.345 48.749 1.855 1.00 38.89 O ATOM 138 N THRA1022 15.586 46.810 1.029 1.00 39.74 N ATOM 139 CA THR A1022 15.67047.244 −0.350 1.00 40.51 C ATOM 140 CB THR A1022 15.220 46.117 −1.3001.00 40.54 C ATOM 141 OG1 THR A1022 15.975 44.930 −1.019 1.00 40.47 OATOM 142 CG2 THR A1022 15.442 46.525 −2.753 1.00 41.07 C ATOM 143 C THRA1022 14.795 48.472 −0.579 1.00 40.85 C ATOM 144 O THR A1022 15.22749.433 −1.204 1.00 41.01 O ATOM 145 N ARG A1023 13.577 48.442 −0.0481.00 41.28 N ATOM 146 CA ARG A1023 12.626 49.541 −0.215 1.00 41.51 CATOM 147 CB ARG A1023 11.198 49.003 −0.083 1.00 41.55 C ATOM 148 CG ARGA1023 10.804 48.042 −1.201 1.00 42.10 C ATOM 149 CD ARG A1023 9.46047.375 −0.938 1.00 42.16 C ATOM 150 NE ARG A1023 8.439 48.328 −0.5140.05 42.12 N ATOM 151 CZ ARG A1023 7.158 48.021 −0.344 0.05 42.14 C ATOM152 NH1 ARG A1023 6.734 46.785 −0.567 0.05 42.17 N ATOM 153 NH2 ARGA1023 6.300 48.947 0.061 0.05 42.16 N ATOM 154 C ARG A1023 12.798 50.7470.710 1.00 41.61 C ATOM 155 O ARG A1023 12.396 51.851 0.363 1.00 41.34 OATOM 156 N HIS A1024 13.395 50.544 1.878 1.00 42.27 N ATOM 157 CA HISA1024 13.583 51.636 2.835 1.00 42.70 C ATOM 158 CB HIS A1024 12.65851.445 4.040 0.05 42.61 C ATOM 159 CG HIS A1024 11.202 51.471 3.693 0.0542.54 C ATOM 160 CD2 HIS A1024 10.233 50.537 3.841 0.05 42.53 C ATOM 161ND1 HIS A1024 10.592 52.567 3.121 0.05 42.51 N ATOM 162 CE1 HIS A10249.311 52.307 2.932 0.05 42.49 C ATOM 163 NE2 HIS A1024 9.067 51.0813.360 0.05 42.48 N ATOM 164 C HIS A1024 15.028 51.727 3.307 1.00 43.14 CATOM 165 O HIS A1024 15.483 50.930 4.131 1.00 43.24 O ATOM 166 N GLUA1025 15.732 52.722 2.782 1.00 43.47 N ATOM 167 CA GLU A1025 17.13952.963 3.089 1.00 43.74 C ATOM 168 CB GLU A1025 17.596 54.249 2.393 1.0044.50 C ATOM 169 CG GLU A1025 17.396 54.230 0.888 1.00 45.87 C ATOM 170CD GLU A1025 18.031 55.420 0.208 1.00 46.86 C ATOM 171 OE1 GLU A102519.267 55.571 0.320 1.00 47.25 O ATOM 172 OE2 GLU A1025 17.294 56.201−0.434 1.00 47.49 O ATOM 173 C GLU A1025 17.539 53.030 4.565 1.00 43.28C ATOM 174 O GLU A1025 18.655 52.645 4.912 1.00 43.56 O ATOM 175 N GLYA1026 16.649 53.523 5.424 1.00 42.64 N ATOM 176 CA GLY A1026 16.97253.631 6.838 1.00 41.75 C ATOM 177 C GLY A1026 16.244 52.645 7.731 1.0041.40 C ATOM 178 O GLY A1026 16.091 52.877 8.931 1.00 41.35 O ATOM 179 NPHE A1027 15.801 51.537 7.144 1.00 40.74 N ATOM 180 CA PHE A1027 15.07750.500 7.871 1.00 39.69 C ATOM 181 CB PHE A1027 14.695 49.376 6.906 1.0039.76 C ATOM 182 CG PHE A1027 13.976 48.233 7.558 1.00 40.05 C ATOM 183CD1 PHE A1027 12.654 48.369 7.978 1.00 40.03 C ATOM 184 CD2 PHE A102714.618 47.012 7.748 1.00 39.83 C ATOM 185 CE1 PHE A1027 11.982 47.3018.576 1.00 39.93 C ATOM 186 CE2 PHE A1027 13.955 45.944 8.344 1.00 39.71C ATOM 187 CZ PHE A1027 12.636 46.089 8.757 1.00 39.70 C ATOM 188 C PHEA1027 15.900 49.920 9.020 1.00 39.08 C ATOM 189 O PHE A1027 15.47049.929 10.175 1.00 38.67 O ATOM 190 N ALA A1028 17.080 49.409 8.682 1.0038.48 N ATOM 191 CA ALA A1028 17.980 48.811 9.656 1.00 38.36 C ATOM 192CB ALA A1028 19.242 48.321 8.960 1.00 37.96 C ATOM 193 C ALA A102818.349 49.784 10.764 1.00 38.25 C ATOM 194 O ALA A1028 18.533 49.38411.907 1.00 38.15 O ATOM 195 N LYS A1029 18.456 51.061 10.418 1.00 38.38N ATOM 196 CA LYS A1029 18.823 52.094 11.380 1.00 38.44 C ATOM 197 CBLYS A1029 19.154 53.391 10.636 1.00 39.34 C ATOM 198 CG LYS A1029 19.99754.393 11.411 1.00 40.55 C ATOM 199 CD LYS A1029 19.248 55.005 12.5911.00 41.77 C ATOM 200 CE LYS A1029 20.043 56.146 13.215 1.00 41.81 CATOM 201 NZ LYS A1029 20.282 57.218 12.208 1.00 42.20 N ATOM 202 C LYSA1029 17.703 52.331 12.386 1.00 37.98 C ATOM 203 O LYS A1029 17.94852.731 13.522 1.00 38.26 O ATOM 204 N ARG A1030 16.470 52.084 11.9691.00 37.55 N ATOM 205 CA ARG A1030 15.330 52.267 12.856 1.00 37.18 CATOM 206 CB ARG A1030 14.050 52.489 12.040 1.00 38.15 C ATOM 207 CG ARGA1030 13.833 53.934 11.573 1.00 39.87 C ATOM 208 CD ARG A1030 12.44954.110 10.937 1.00 40.62 C ATOM 209 NE ARG A1030 12.383 53.532 9.5981.00 41.54 N ATOM 210 CZ ARG A1030 12.825 54.142 8.500 1.00 42.11 C ATOM211 NH1 ARG A1030 13.359 55.355 8.577 1.00 41.94 N ATOM 212 NH2 ARGA1030 12.747 53.533 7.323 1.00 42.66 N ATOM 213 C ARG A1030 15.14551.064 13.780 1.00 36.44 C ATOM 214 O ARG A1030 14.650 51.202 14.9001.00 36.62 O ATOM 215 N VAL A1031 15.560 49.889 13.313 1.00 35.30 N ATOM216 CA VAL A1031 15.417 48.655 14.080 1.00 34.12 C ATOM 217 CB VAL A103115.160 47.458 13.145 1.00 34.29 C ATOM 218 CG1 VAL A1031 14.965 46.19013.963 1.00 34.93 C ATOM 219 CG2 VAL A1031 13.949 47.723 12.279 1.0034.77 C ATOM 220 C VAL A1031 16.615 48.300 14.960 1.00 33.18 C ATOM 221O VAL A1031 16.447 47.763 16.057 1.00 33.04 O ATOM 222 N LEU A103217.818 48.595 14.482 1.00 31.96 N ATOM 223 CA LEU A1032 19.026 48.26415.226 1.00 31.28 C ATOM 224 CB LEU A1032 20.081 47.692 14.274 1.0030.83 C ATOM 225 CG LEU A1032 19.665 46.475 13.438 1.00 30.70 C ATOM 226CD1 LEU A1032 20.852 46.007 12.608 1.00 30.16 C ATOM 227 CD2 LEU A103219.172 45.351 14.349 1.00 30.17 C ATOM 228 C LEU A1032 19.634 49.42216.005 1.00 30.91 C ATOM 229 O LEU A1032 19.534 50.578 15.602 1.00 31.10O ATOM 230 N THR A1033 20.262 49.095 17.129 1.00 30.41 N ATOM 231 CA THRA1033 20.918 50.094 17.960 1.00 29.93 C ATOM 232 CB THR A1033 21.11349.605 19.410 1.00 29.26 C ATOM 233 OG1 THR A1033 22.084 48.552 19.4381.00 28.24 O ATOM 234 CG2 THR A1033 19.800 49.097 19.980 1.00 29.31 CATOM 235 C THR A1033 22.291 50.334 17.339 1.00 30.14 C ATOM 236 O THRA1033 22.678 49.633 16.405 1.00 29.45 O ATOM 237 N ALA A1034 23.01851.321 17.856 1.00 30.49 N ATOM 238 CA ALA A1034 24.344 5L638 17.3391.00 31.05 C ATOM 239 CB ALA A1034 24.987 52.734 18.177 1.00 30.92 CATOM 240 C ALA A1034 25.211 50.388 17.356 1.00 31.28 C ATOM 241 O ALAA1034 25.837 50.047 16.357 1.00 31.20 O ATOM 242 N LEU A1035 25.24149.706 18.495 1.00 31.90 N ATOM 243 CA LEU A1035 26.030 48.487 18.6191.00 32.66 C ATOM 244 CB LEU A1035 25.878 47.907 20.031 1.00 32.74 CATOM 245 CG LEU A1035 26.464 48.733 21.195 1.00 32.90 C ATOM 246 CD1 LEUA1035 26.003 48.158 22.529 1.00 32.38 C ATOM 247 CD2 LEU A1035 27.98548.737 21.121 1.00 32.56 C ATOM 248 C LEU A1035 25.612 47.454 17.5561.00 33.36 C ATOM 249 O LEU A1035 26.442 46.992 16.769 1.00 33.53 O ATOM250 N GLU A1036 24.328 47.104 17.526 1.00 33.64 N ATOM 251 CA GLU A103623.822 46.140 16.555 1.00 34.14 C ATOM 252 CB GLU A1036 22.299 46.01416.682 1.00 33.87 C ATOM 253 CG GLU A1036 21.818 45.217 17.890 1.0033.65 C ATOM 254 CD GLU A1036 20.341 45.462 18.216 1.00 33.37 C ATOM 255OE1 GLU A1036 19.726 44.613 18.895 1.00 32.88 O ATOM 256 OE2 GLU A103619.797 46.509 17.808 1.00 33.01 O ATOM 257 C GLU A1036 24.188 46.57315.137 1.00 34.85 C ATOM 258 O GLU A1036 24.526 45.752 14.284 1.00 34.59O ATOM 259 N MET A1037 24.120 47.875 14.893 1.00 35.84 N ATOM 260 CA META1037 24.436 48.433 13.585 1.00 37.02 C ATOM 261 CB MET A1037 24.17249.936 13.605 1.00 37.11 C ATOM 262 CG MET A1037 23.656 50.510 12.2941.00 38.16 C ATOM 263 SD MET A1037 22.148 49.717 11.685 1.00 38.53 SATOM 264 CE MET A1037 22.507 49.661 9.949 1.00 38.71 C ATOM 265 C META1037 25.899 48.141 13.215 1.00 37.76 C ATOM 266 O MET A1037 26.22747.928 12.044 1.00 37.71 O ATOM 267 N GLU A1038 26.774 48.117 14.2171.00 38.51 N ATOM 268 CA GLU A1038 28.183 47.835 13.977 1.00 39.30 CATOM 269 CB GLU A1038 28.989 47.966 15.275 1.00 40.38 C ATOM 270 CG GLUA1038 28.963 49.369 15.880 1.00 41.32 C ATOM 271 CD GLU A1038 29.87449.513 17.086 1.00 42.00 C ATOM 272 OE1 GLU A1038 29.789 50.553 17.7711.00 42.33 O ATOM 273 OE2 GLU A1038 30.677 48.592 17.349 1.00 42.44 OATOM 274 C GLU A1038 28.349 46.436 13.395 1.00 39.50 C ATOM 275 O GLUA1038 28.932 46.272 12.327 1.00 40.05 O ATOM 276 N ARG A1039 27.83745.423 14.087 1.00 39.36 N ATOM 277 CA ARG A1039 27.945 44.063 13.5771.00 39.25 C ATOM 278 CB ARG A1039 27.347 43.053 14.563 1.00 39.62 CATOM 279 CG ARG A1039 27.395 41.632 14.025 1.00 40.25 C ATOM 280 CD ARGA1039 27.177 40.585 15.089 1.00 40.85 C ATOM 281 NE ARG A1039 27.25139.243 14.516 1.00 41.68 N ATOM 282 CZ ARG A1039 28.314 38.756 13.8791.00 42.00 C ATOM 283 NH1 ARG A1039 28.289 37.523 13.387 1.00 42.01 NATOM 284 NH2 ARG A1039 29.408 39.496 13.735 1.00 41.92 N ATOM 285 C ARGA1039 27.241 43.938 12.228 1.00 39.03 C ATOM 286 O ARG A1039 27.77443.347 11.291 1.00 38.64 O ATOM 287 N PHE A1040 26.040 44.502 12.1361.00 39.10 N ATOM 288 CA PHE A1040 25.255 44.464 10.901 1.00 39.18 CATOM 289 CB PHE A1040 24.030 45.369 11.036 1.00 38.05 C ATOM 290 CG PHEA1040 23.268 45.560 9.754 1.00 37.43 C ATOM 291 CD1 PHE A1040 22.44344.557 9.258 1.00 37.16 C ATOM 292 CD2 PHE A1040 23.365 46.752 9.0451.00 37.16 C ATOM 293 CE1 PHE A1040 21.722 44.742 8.074 1.00 36.76 CATOM 294 CE2 PHE A1040 22.649 46.946 7.863 1.00 36.76 C ATOM 295 CZ PHEA1040 21.825 45.936 7.379 1.00 36.61 C ATOM 296 C PHE A1040 26.06344.910 9.682 1.00 39.84 C ATOM 297 O PHE A1040 26.157 44.190 8.682 1.0039.67 O ATOM 298 N THR A1041 26.643 46.104 9.774 1.00 40.57 N ATOM 299CA THR A1041 27.415 46.668 8.676 1.00 41.24 C ATOM 300 CB THR A104127.726 48.138 8.938 1.00 41.14 C ATOM 301 OG1 THR A1041 28.364 48.27210.212 1.00 41.93 O ATOM 302 CG2 THR A1041 26.446 48.948 8.933 1.0040.95 C ATOM 303 C THR A1041 28.708 45.931 8.353 1.00 41.72 C ATOM 304 OTHR A1041 29.251 46.080 7.259 1.00 41.99 O ATOM 305 N SER A1042 29.19845.133 9.297 1.00 42.15 N ATOM 306 CA SER A1042 30.419 44.367 9.078 1.0042.65 C ATOM 307 CB SER A1042 31.106 44.057 10.407 1.00 42.64 C ATOM 308OG SER A1042 30.642 42.828 10.934 1.00 43.03 O ATOM 309 C SER A104230.066 43.050 8.381 1.00 43.22 C ATOM 310 O SER A1042 30.937 42.2188.118 1.00 43.14 O ATOM 311 N LEU A1043 28.781 42.869 8.095 1.00 43.80 NATOM 312 CA LEU A1043 28.298 41.660 7.439 1.00 44.32 C ATOM 313 CB LEUA1043 27.151 41.040 8.247 1.00 43.98 C ATOM 314 CG LEU A1043 27.49140.512 9.642 1.00 43.88 C ATOM 315 CD1 LEU A1043 26.219 40.165 10.3881.00 43.76 C ATOM 316 CD2 LEU A1043 28.383 39.294 9.521 1.00 44.03 CATOM 317 C LEU A1043 27.821 41.973 6.026 1.00 44.90 C ATOM 318 O LEUA1043 27.448 43.110 5.722 1.00 44.88 O ATOM 319 N LYS A1044 27.82740.950 5.174 1.00 45.38 N ATOM 320 CA LYS A1044 27.412 41.088 3.782 1.0045.95 C ATOM 321 CB LYS A1044 28.556 40.673 2.856 1.00 46.91 C ATOM 322CG LYS A1044 28.976 39.209 3.060 1.00 47.97 C ATOM 323 CD LYS A104429.803 38.669 1.896 1.00 48.98 C ATOM 324 CE LYS A1044 30.319 37.2602.187 1.00 49.35 C ATOM 325 NZ LYS A1044 29.216 36.313 2.505 1.00 49.24N ATOM 326 C LYS A1044 26.202 40.217 3.457 1.00 45.75 C ATOM 327 O LYSA1044 25.779 39.391 4.266 1.00 46.06 O ATOM 328 N GLY A1045 25.67440.416 2.252 1.00 45.39 N ATOM 329 CA GLY A1045 24.538 39.663 1.743 1.0044.96 C ATOM 330 C GLY A1045 23.577 38.960 2.685 1.00 44.52 C ATOM 331 OGLY A1045 23.147 39.520 3.692 1.00 44.43 O ATOM 332 N ARG A1046 23.23137.726 2.333 1.00 44.21 N ATOM 333 CA ARG A1046 22.297 36.917 3.112 1.0043.89 C ATOM 334 CB ARG A1046 22.304 35.474 2.589 1.00 44.58 C ATOM 335CG ARG A1046 21.962 35.399 1.099 1.00 46.46 C ATOM 336 CD ARG A104621.891 33.977 0.547 1.00 47.97 C ATOM 337 NE ARG A1046 20.698 33.2530.979 1.00 49.25 N ATOM 338 CZ ARG A1046 20.360 32.043 0.538 1.00 49.83C ATOM 339 NH1 ARG A1046 19.257 31.454 0.983 1.00 49.98 N ATOM 340 NH2ARG A1046 21.123 31.420 −0.352 1.00 49.87 N ATOM 341 C ARG A1046 22.57236.951 4.609 1.00 43.05 C ATOM 342 O ARG A1046 21.657 37.167 5.402 1.0042.92 O ATOM 343 N ARG A1047 23.830 36.751 4.994 1.00 42.04 N ATOM 344CA ARG A1047 24.212 36.775 6.401 1.00 40.92 C ATOM 345 CB ARG A104725.726 36.592 6.553 1.00 41.86 C ATOM 346 CG ARG A1047 26.196 35.1466.581 1.00 43.21 C ATOM 347 CD ARG A1047 27.613 35.070 7.134 1.00 44.61C ATOM 348 NE ARG A1047 28.023 33.709 7.475 1.00 45.70 N ATOM 349 CZ ARGA1047 28.346 32.773 6.588 1.00 46.26 C ATOM 350 NH1 ARG A1047 28.70531.565 7.004 1.00 46.85 N ATOM 351 NH2 ARG A1047 28.318 33.042 5.2891.00 46.67 N ATOM 352 C ARG A1047 23.800 38.082 7.074 1.00 39.44 C ATOM353 O ARG A1047 23.397 38.100 8.236 1.00 38.89 O ATOM 354 N GLN A104823.914 39.178 6.338 1.00 37.81 N ATOM 355 CA GLN A1048 23.550 40.4756.871 1.00 36.41 C ATOM 356 CB GLN A1048 24.011 41.576 5.920 1.00 36.74C ATOM 357 CG GLN A1048 24.106 42.940 6.565 1.00 37.57 C ATOM 358 CD GLNA1048 24.476 44.024 5.578 1.00 38.09 C ATOM 359 OE1 GLN A1048 24.86045.132 5.965 1.00 38.67 O ATOM 360 NE2 CLN A1048 24.351 43.717 4.2951.00 38.03 N ATOM 361 C GLN A1048 22.037 40.561 7.074 1.00 35.21 C ATOM362 O GLN A1048 21.567 41.201 8.015 1.00 34.68 O ATOM 363 N ILE A104921.279 39.919 6.189 1.00 33.75 N ATOM 364 CA ILE A1049 19.826 39.9346.295 1.00 32.76 C ATOM 365 CB ILE A1049 19.146 39.436 4.987 1.00 32.88C ATOM 366 CG2 ILE A1049 17.628 39.437 5.153 1.00 32.63 C ATOM 367 CG1ILE A1049 19.536 40.333 3.808 1.00 32.63 C ATOM 368 CD1 ILE A1049 19.07041.776 3.930 1.00 32.59 C ATOM 369 C ILE A1049 19.366 39.062 7.466 1.0031.99 C ATOM 370 O ILE A1049 18.480 39.456 8.223 1.00 31.76 O ATOM 371 NGLU A1050 19.964 37.883 7.611 1.00 31.37 N ATOM 372 CA GLU A1050 19.61036.982 8.707 1.00 31.34 C ATOM 373 CB GLU A1050 20.362 35.648 8.591 1.0032.61 C ATOM 374 CG GLU A1050 20.706 34.980 9.944 1.00 36.11 C ATOM 375CD GLU A1050 19.482 34.642 10.819 1.00 37.78 C ATOM 376 OE1 GLU A105019.674 34.340 12.024 1.00 39.05 O ATOM 377 OE2 GLU A1050 18.339 34.67110.311 1.00 38.44 O ATOM 378 C GLU A1050 19.929 37.642 10.047 1.00 30.27C ATOM 379 O GLU A1050 19.172 37.494 11.014 1.00 30.09 O ATOM 380 N TYRA1051 21.041 38.372 10.107 1.00 28.49 N ATOM 381 CA TYR A1051 21.39839.040 11.343 1.00 27.23 C ATOM 382 CB TYR A1051 22.747 39.750 11.2441.00 26.82 C ATOM 383 CG TYR A1051 23.032 40.565 12.484 1.00 26.72 CATOM 384 CD1 TYR A1051 22.657 41.906 12.569 1.00 26.89 C ATOM 385 CE1TYR A1051 22.830 42.627 13.750 1.00 26.37 C ATOM 386 CD2 TYR A105123.590 39.970 13.612 1.00 26.66 C ATOM 387 CE2 TYR A1051 23.761 40.67614.786 1.00 26.28 C ATOM 388 CZ TYR A1051 23.381 42.000 14.852 1.0026.29 C ATOM 389 OH TYR A1051 23.554 42.688 16.031 1.00 26.92 O ATOM 390C TYR A1051 20.332 40.069 11.670 1.00 26.31 C ATOM 391 O TYR A105119.893 40.189 12.811 1.00 25.81 O ATOM 392 N LEU A1052 19.927 40.81210.650 1.00 25.22 N ATOM 393 CA LEU A1052 18.923 41.845 10.809 1.0024.40 C ATOM 394 CB LEU A1052 18.854 42.685 9.532 1.00 24.44 C ATOM 395CG LEU A1052 17.719 43.703 9.465 1.00 25.24 C ATOM 396 CD1 LEU A105217.904 44.780 10.533 1.00 24.85 C ATOM 397 CD2 LEU A1052 17.692 44.3148.081 1.00 25.55 C ATOM 398 C LEU A1052 17.551 41.242 11.126 1.00 23.78C ATOM 399 O LEU A1052 16.808 41.771 11.957 1.00 23.28 O ATOM 400 N ALAA1053 17.227 40.134 10.459 1.00 22.87 N ATOM 401 CA ALA A1053 15.94839.459 10.655 1.00 22.13 C ATOM 402 CB ALA A1053 15.780 38.354 9.6191.00 21.79 C ATOM 403 C ALA A1053 15.858 38.875 12.066 1.00 21.81 C ATOM404 O ALA A1053 14.841 39.022 12.748 1.00 21.24 O ATOM 405 N GLY A105416.932 38.215 12.497 1.00 21.35 N ATOM 406 CA GLY A1054 16.953 37.62413.819 1.00 20.95 C ATOM 407 C GLY A1054 16.707 38.649 14.910 1.00 20.80C ATOM 408 O GLY A1054 15.890 38.428 15.803 1.00 20.64 O ATOM 409 N ARGA1055 17.419 39.769 14.845 1.00 20.73 N ATOM 410 CA ARG A1055 17.25540.822 15.843 1.00 21.15 C ATOM 411 CB ARG A1055 18.254 41.959 15.5861.00 20.76 C ATOM 412 CG ARG A1055 19.514 41.893 16.444 1.00 20.45 CATOM 413 CD ARG A1055 20.238 40.562 16.281 1.00 20.93 C ATOM 414 NE ARGA1055 21.323 40.413 17.249 1.00 20.92 N ATOM 415 CZ ARG A1055 22.10939.344 17.337 1.00 21.08 C ATOM 416 NH1 ARG A1055 21.937 38.314 16.5151.00 21.54 N ATOM 417 NH2 ARG A1055 23.073 39.308 18.246 1.00 20.48 NATOM 418 C ARG A1055 15.822 41.355 15.834 1.00 20.82 C ATOM 419 O ARGA1055 15.235 41.597 16.884 1.00 19.96 O ATOM 420 N TRP A1056 15.27241.535 14.638 1.00 21.33 N ATOM 421 CA TRP A1056 13.907 42.018 14.4811.00 21.83 C ATOM 422 CB TRP A1056 13.597 42.252 12.995 1.00 23.26 CATOM 423 CG TRP A1056 12.117 42.342 12.688 1.00 25.60 C ATOM 424 CD2 TRPA1056 11.384 43.518 12.326 1.00 26.69 C ATOM 425 CE2 TRP A1056 10.02643.140 12.186 1.00 27.05 C ATOM 426 CE3 TRP A1056 11.741 44.852 12.1061.00 27.71 C ATOM 427 CD1 TRP A1056 11.199 41.324 12.745 1.00 26.25 CATOM 428 NE1 TRP A1056 9.942 41.798 12.448 1.00 27.38 N ATOM 429 CZ2 TRPA1056 9.025 44.048 11.839 1.00 28.05 C ATOM 430 CZ3 TRP A1056 10.74145.763 11.757 1.00 29.41 C ATOM 431 CH2 TRP A1056 9.397 45.353 11.6281.00 28.81 C ATOM 432 C TRP A1056 12.956 40.973 15.059 1.00 21.40 C ATOM433 O TRP A1056 11.999 41.299 15.754 1.00 21.32 O ATOM 434 N SER A105713.233 39.714 14.752 1.00 20.70 N ATOM 435 CA SER A1057 12.429 38.60515.231 1.00 20.76 C ATOM 436 CB SER A1057 12.956 37.293 14.632 1.0021.29 C ATOM 437 OG SER A1057 12.032 36.234 14.815 1.00 23.54 O ATOM 438C SER A1057 12.498 38.559 16.760 1.00 20.11 C ATOM 439 O SER A105711.484 38.361 17.438 1.00 19.93 O ATOM 440 N ALA A1058 13,693 38.75017.303 1.00 19.35 N ATOM 441 CA ALA A1058 13.881 38.727 18.751 1.0018.89 C ATOM 442 CB ALA A1058 15.373 38.780 19.098 1.00 18.02 C ATOM 443C ALA A1058 13.139 39.865 19.448 1.00 18.51 C ATOM 444 O ALA A105812.502 39.657 20.482 1.00 17.31 O ATOM 445 N LYS A1059 13.213 41.06218.875 1.00 19.01 N ATOM 446 CA LYS A1059 12.560 42.230 19.470 1.0020.07 C ATOM 447 CB LYS A1059 13.026 43.513 18.771 1.00 19.92 C ATOM 448CG LYS A1059 14.539 43.671 18.811 1.00 20.81 C ATOM 449 CD LYS A105915.003 45.101 18.534 1.00 21.35 C ATOM 450 CE LYS A1059 16.530 45.19018.538 1.00 21.30 C ATOM 451 NZ LYS A1059 17.028 46.597 18.453 1.0021.29 N ATOM 452 C LYS A1059 11.045 42.112 19.420 1.00 20.60 C ATOM 453O LYS A1059 10.341 42.601 20.309 1.00 19.75 O ATOM 454 N GLU A106010.550 41.448 18.381 1.00 21.44 N ATOM 455 CA GLU A1060 9.118 41.24618.234 1.00 22.69 C ATOM 456 CB GLU A1060 8.783 40.742 16.832 1.00 24.22C ATOM 457 CG GLU A1060 7.303 40.761 16.521 1.00 27.42 C ATOM 458 CD GLUA1060 6.730 42.169 16.542 1.00 29.59 C ATOM 459 OE1 GLU A1060 7.31443.053 15.866 1.00 29.73 O ATOM 460 OE2 GLU A1060 5.700 42.386 17.2291.00 30.63 O ATOM 461 C GLU A1060 8.651 40.220 19.263 1.00 22.63 C ATOM462 O GLU A1060 7.631 40.418 19.932 1.00 22.87 O ATOM 463 N ALA A10619.395 39.125 19.391 1.00 22.05 N ATOM 464 CA ALA A1061 9.012 38.09120.346 1.00 22.06 C ATOM 465 CB ALA A1061 9.967 36.899 20.266 1.00 21.94C ATOM 466 C ALA A1061 8.997 38.663 21.755 1.00 22.04 C ATOM 467 O ALAA1061 8.106 38.359 22.539 1.00 21.13 O ATOM 468 N PHE A1062 9.978 39.50622.063 1.00 22.38 N ATOM 469 CA PHE A1062 10.055 40.119 23.380 1.0023.29 C ATOM 470 CB PHE A1062 11.348 40.918 23.532 1.00 22.75 C ATOM 471CG PHE A1062 11.440 41.648 24.833 1.00 22.71 C ATOM 472 CD1 PHE A106210.804 42.876 25.003 1.00 22.28 C ATOM 473 CD2 PHE A1062 12.107 41.08025.914 1.00 22.60 C ATOM 474 CE1 PHE A1062 10.828 43.529 26.232 1.0022.88 C ATOM 475 CE2 PHE A1062 12.138 41.722 27.154 1.00 22.54 C ATOM476 CZ PHE A1062 11.497 42.951 27.314 1.00 22.78 C ATOM 477 C PHE A10628.865 41.030 23.667 1.00 24.27 C ATOM 478 O PHE A1062 8.302 41.00224.765 1.00 24.37 O ATOM 479 N SER A1063 8.498 41.843 22.681 1.00 25.39N ATOM 480 CA SER A1063 7.373 42.751 22.818 1.00 26.79 C ATOM 481 CB SERA1063 7.196 43.580 21.542 1.00 27.55 C ATOM 482 OG SER A1063 8.18444.598 21.464 1.00 28.80 O ATOM 483 C SER A1063 6.108 41.965 23.094 1.0027.26 C ATOM 484 O SER A1063 5.271 42.366 23.897 1.00 27.47 O ATOM 485 NLYS A1064 5.963 40.840 22.421 1.00 28.03 N ATOM 486 CA LYS A1064 4.79340.018 22.637 1.00 29.08 C ATOM 487 CB LYS A1064 4.725 38.936 21.5661.00 28.90 C ATOM 488 CG LYS A1064 4.426 39.521 20.195 1.00 30.31 C ATOM489 CD LYS A1064 4.605 38.519 19.075 1.00 31.26 C ATOM 490 CE LYS A10643.733 37.309 19.269 1.00 32.24 C ATOM 491 NZ LYS A1064 3.887 36.36118.141 1.00 33.56 N ATOM 492 C LYS A1064 4.866 39.428 24.043 1.00 29.71C ATOM 493 O LYS A1064 3.886 39.467 24.788 1.00 29.61 O ATOM 494 N ALAA1065 6.043 38.926 24.413 1.00 30.48 N ATOM 495 CA ALA A1065 6.26338.341 25.732 1.00 31.56 C ATOM 496 CB ALA A1065 7.739 38.022 25.9171.00 31.00 C ATOM 497 C ALA A1065 5.780 39.269 26.851 1.00 32.65 C ATOM498 O ALA A1065 5.300 38.807 27.882 1.00 31.64 O ATOM 499 N MET A10665.922 40.574 26.646 1.00 34.63 N ATOM 500 CA MET A1066 5.479 41.55727.630 1.00 37.05 C ATOM 501 CB MET A1066 6.245 42.874 27.458 1.00 37.61C ATOM 502 CG MET A1066 7.710 42.808 27.867 1.00 39.52 C ATOM 503 SD META1066 8.007 43.039 29.649 1.00 41.34 S ATOM 504 CE MET A1066 8.98344.550 29.647 1.00 40.03 C ATOM 505 C MET A1066 3.985 41.798 27.435 1.0038.24 C ATOM 506 O MET A1066 3.313 42.364 28.295 1.00 38.31 O ATOM 507 NGLY A1067 3.473 41.353 26.293 1.00 39.97 N ATOM 508 CA GLY A1067 2.06541.524 25.996 1.00 42.23 C ATOM 509 C GLY A1067 1.716 42.953 25.623 1.0043.61 C ATOM 510 O GLY A1067 1.055 43.658 26.383 1.00 44.09 O ATOM 511 NTHR A1068 2.167 43.387 24,452 1.00 44.84 N ATOM 512 CA THR A1068 1.88944.739 23.985 1.00 46.14 C ATOM 513 CB THR A1068 3.165 45.419 23.4441.00 45.80 C ATOM 514 OG1 THR A1068 3.639 44.703 22.297 1.00 45.63 OATOM 515 CG2 THR A1068 4.249 45.434 24.500 1.00 45.44 C ATOM 516 C THRA1068 0.854 44.654 22.868 1.00 47.39 C ATOM 517 O THR A1068 0.473 45.66122.270 1.00 47.66 O ATOM 518 N GLY A1069 0.409 43.432 22.592 1.00 48.83N ATOM 519 CA GLY A1069 0.585 43.211 21.555 1.00 50.40 C ATOM 520 C GLYA1069 0.073 43.511 20.162 1.00 51.38 C ATOM 521 O GLY A1069 0.661 42.71619.569 1.00 51.45 O ATOM 522 N ILE A1070 0.473 44.665 19.637 1.00 52.38N ATOM 523 CA ILE A1070 0.061 45.102 18.308 1.00 53.00 C ATOM 524 CB ILEA1070 1.285 45.483 17.444 1.00 53.24 C ATOM 525 CG2 ILE A1070 2.14844.245 17.194 1.00 53.03 C ATOM 526 CG1 ILE A1070 2.102 46.575 18.1451.00 53.21 C ATOM 527 CD1 ILE A1070 3.310 47.043 17.350 1.00 53.51 CATOM 528 C ILE A1070 0.850 46.316 18.471 1.00 53.30 C ATOM 529 O ILEA1070 1.800 46.506 17.705 1.00 53.48 O ATOM 530 N SER A1071 0.544 47.13719.473 1.00 53.35 N ATOM 531 CA SER A1071 1.344 48.321 19.771 1.00 53.45C ATOM 532 CB SER A1071 0.643 49.183 20.816 1.00 53.58 C ATOM 533 OG SERA1071 0.577 48.494 22.058 1.00 54.00 O ATOM 534 C SER A1071 2.631 47.76520.360 1.00 53.38 C ATOM 535 O SER A1071 2.596 46.720 21.019 1.00 53.61O ATOM 536 N LYS A1072 3.763 48.431 20.138 1.00 52.81 N ATOM 537 CA LYSA1072 5.019 47.908 20.680 1.00 52.05 C ATOM 538 CB LYS A1072 5.85747.243 19.575 1.00 52.53 C ATOM 539 CG LYS A1072 5.068 46.578 18.4591.00 53.49 C ATOM 540 CD LYS A1072 4.079 45.535 18.964 1.00 54.32 C ATOM541 CE LYS A1072 4.750 44.344 19.619 1.00 54.90 C ATOM 542 NZ LYS A10723.722 43.377 20.117 1.00 55.42 N ATOM 543 C LYS A1072 5.897 48.93621.383 1.00 51.05 C ATOM 544 O LYS A1072 5.587 50.127 21.442 1.00 50.60O ATOM 545 N LEU A1073 7.002 48.435 21.923 1.00 50.01 N ATOM 546 CA LEUA1073 7.989 49.254 22.599 1.00 48.81 C ATOM 547 CB LEU A1073 8.78548.409 23.601 1.00 49.31 C ATOM 548 CG LEU A1073 8.166 48.084 24.9691.00 49.63 C ATOM 549 CD1 LEU A1073 6.806 47,433 24.812 1.00 49.83 CATOM 550 CD2 LEU A1073 9.099 47.160 25.720 1.00 50.04 C ATOM 551 C LEUA1073 8.930 49.779 21.521 1.00 47.79 C ATOM 552 O LEU A1073 8.923 49.29420.383 1.00 47.71 O ATOM 553 N GLY A1074 9.733 50.776 21.869 1.00 46.44N ATOM 554 CA GLY A1074 10.670 51.301 20.896 1.00 44.58 C ATOM 555 C GLYA1074 11.722 50.244 20.621 1.00 43.12 C ATOM 556 O GLY A1074 12.31549.697 21.553 1.00 43.10 O ATOM 557 N PHE A1075 11.949 49.934 19.3511.00 41.71 N ATOM 558 CA PHE A1075 12.949 48.937 19.006 1.00 40.26 CATOM 559 CB PHE A1075 12.870 48.613 17.514 1.00 41.07 C ATOM 560 CG PHEA1075 11.958 47.459 17.207 1.00 42.00 C ATOM 561 CD1 PHE A1075 10.93047.112 18.096 1.00 42.62 C ATOM 562 CD2 PHE A1075 12.124 46.707 16.0481.00 42.28 C ATOM 563 CE1 PHE A1075 10.081 46.026 17.835 1.00 42.81 CATOM 564 CE2 PHE A1075 11.281 45.617 15.771 1.00 42.42 C ATOM 565 CZ PHEA1075 10.261 45.276 16.666 1.00 42.86 C ATOM 566 C PHE A1075 14.34649.388 19.413 1.00 38.94 C ATOM 567 O PHE A1075 15.257 48.569 19.5521.00 38.45 O ATOM 568 N GLN A1076 14.503 50.692 19.623 1.00 37.14 N ATOM569 CA GLN A1076 15.779 51.244 20.051 1.00 35.77 C ATOM 570 CB GLN A107615.864 52.739 19.720 1.00 35.98 C ATOM 571 CG GLN A1076 16.064 53.04618.240 1.00 35.74 C ATOM 572 CD GLN A1076 17.323 52.418 17.683 1.0035.92 C ATOM 573 OE1 GLN A1076 18.429 52.672 18.169 1.00 36.68 O ATOM574 NE2 GLN A1076 17.166 51.592 16.659 1.00 35.79 N ATOM 575 C GLN A107615.927 51.043 21.556 1.00 34.84 C ATOM 576 O GLN A1076 17.000 51.24922.116 1.00 34.87 O ATOM 577 N ASP A1077 14.840 50.638 22.202 1.00 33.69N ATOM 578 CA ASP A1077 14.838 50.395 23.641 1.00 32.88 C ATOM 579 CBASP A1077 13.466 50.738 24.229 1.00 34.04 C ATOM 580 CG ASP A1077 13.18352.230 24.220 1.00 35.48 C ATOM 581 OD1 ASP A1077 13.877 52.971 24.9531.00 36.31 O ATOM 582 OD2 ASP A1077 12.269 52.659 23.477 1.00 36.39 OATOM 583 C ASP A1077 15.170 48.935 23.943 1.00 31.37 C ATOM 584 O ASPA1077 15.205 48.517 25.103 1.00 30.93 O ATOM 585 N LEU A1078 15.40848.165 22.889 1.00 29.66 N ATOM 586 CA LEU A1078 15.724 46.753 23.0261.00 28.12 C ATOM 587 CB LEU A1078 14.605 45.907 22.410 1.00 28.40 CATOM 588 CG LEU A1078 13.211 46.138 22.999 1.00 28.65 C ATOM 589 CD1 LEUA1078 12.175 45.297 22.250 1.00 28.42 C ATOM 590 CD2 LEU A1078 13.23245.784 24.485 1.00 28.42 C ATOM 591 C LEU A1078 17.029 46.469 22.3171.00 26.77 C ATOM 592 O LEU A1078 17.256 46.963 21.219 1.00 26.91 O ATOM593 N GLU A1079 17.892 45.683 22.944 1.00 25.48 N ATOM 594 CA GLU A107919.166 45.352 22.330 1.00 24.50 C ATOM 595 CB GLU A1079 20.287 46.20222.921 1.00 24.22 C ATOM 596 CG GLU A1079 21.561 46.128 22.114 1.0023.64 C ATOM 597 CD GLU A1079 22.638 47.051 22.635 1.00 24.07 C ATOM 598QE1 GLU A1079 23.079 46.862 23.791 1.00 23.41 O ATOM 599 OE2 GLU A107923.044 47.967 21.883 1.00 24.29 O ATOM 600 C GLU A1079 19.512 43.88522.488 1.00 23.86 C ATOM 601 O GLU A1079 19.341 43.305 23.560 1.00 23.77O ATOM 602 N VAL A1080 20.003 43.291 21.408 1.00 23.09 N ATOM 603 CA VALA1080 20.377 41.888 21.411 1.00 22.78 C ATOM 604 CB VAL A1080 19.41341.032 20.529 1.00 22.41 C ATOM 605 CG1 VAL A1080 20.005 39.649 20.2841.00 21.10 C ATOM 606 CG2 VAL A1080 18.059 40.893 21.224 1.00 21.12 CATOM 607 C VAL A1080 21.800 41.707 20.909 1.00 23.31 C ATOM 608 O VALA1080 22.102 41.942 19.737 1.00 23.36 O ATOM 609 N LEU A1081 22.67341.292 21.818 1.00 23.52 N ATOM 610 CA LEU A1081 24.066 41.056 21.4881.00 23.32 C ATOM 611 CB LEU A1081 24.968 41.910 22.391 1.00 22.81 CATOM 612 CG LEU A1081 24.725 43.426 22.313 1.00 22.95 C ATOM 613 CD1 LEUA1081 25.680 44.170 23.239 1.00 22.31 C ATOM 614 CD2 LEU A1081 24.91943.902 20.874 1.00 23.08 C ATOM 615 C LEU A1081 24.347 39.576 21.7091.00 23.58 C ATOM 616 O LEU A1081 23.436 38.786 21.981 1.00 22.36 O ATOM617 N ASN A1082 25.614 39.204 21.582 1.00 24.47 N ATOM 618 CA ASN A108226.018 37.826 21.802 1.00 25.10 C ATOM 619 CB ASN A1082 26.745 37.30120.564 1.00 25.30 C ATOM 620 CG ASN A1082 25.798 37.072 19.406 1.0025.42 C ATOM 621 OD1 ASN A1082 24.863 36.277 19.514 1.00 26.33 O ATOM622 ND2 ASN A1082 26.023 37.769 18.299 1.00 25.02 N ATOM 623 C ASN A108226.897 37.774 23.042 1.00 25.09 C ATOM 624 O ASN A1082 27.802 38.58623.197 1.00 24.45 O ATOM 625 N ASN A1083 26.614 36.825 23.932 1.00 26.16N ATOM 626 CA ASN A1083 27.365 36.697 25.180 1.00 26.89 C ATOM 627 CBASN A1083 26.484 36.048 26.264 1.00 26.14 C ATOM 628 CG ASN A1083 26.09434.600 25.952 1.00 25.65 C ATOM 629 OD1 ASN A1083 25.289 34.006 26.6681.00 25.06 O ATOM 630 ND2 ASN A1083 26.665 34.032 24.900 1.00 25.04 NATOM 631 C ASN A1083 28.691 35.953 25.044 1.00 27.81 C ATOM 632 O ASNA1083 29.098 35.595 23.939 1.00 27.57 O ATOM 633 N GLU A1084 29.37335.729 26.162 1.00 29.55 N ATOM 634 CA GLU A1084 30.656 35.041 26.1021.00 31.72 C ATOM 635 CB GLU A1084 31.382 35.091 27.465 1.00 32.66 CATOM 636 CG GLU A1084 30.618 34.574 28.685 1.00 34.91 C ATOM 637 CD GLUA1084 31.407 34.752 29.998 1.00 36.48 C ATOM 638 OE1 GLU A1084 32.42134.051 30.192 1.00 37.32 O ATOM 639 OE2 GLU A1084 31.022 35.601 30.8411.00 37.46 O ATOM 640 C GLU A1084 30.532 33.603 25.584 1.00 32.13 C ATOM641 O GLU A1084 31.522 33.007 25.186 1.00 32.93 O ATOM 642 N ARG A108529.322 33.052 25.578 1.00 32.33 N ATOM 643 CA ARG A1085 29.118 31.70325.061 1.00 32.71 C ATOM 644 CB ARG A1085 28.057 30.950 25.866 1.0034.65 C ATOM 645 CG ARG A1085 28.525 30.506 27.238 1.00 37.26 C ATOM 646CD ARG A1085 29.588 29.432 27.112 1.00 39.70 C ATOM 647 NE ARG A108530.430 29.337 28.303 1.00 42.39 N ATOM 648 CZ ARG A1085 31.329 28.37528.501 1.00 43.44 C ATOM 649 NH1 ARG A1085 32.062 28.363 29.611 1.0044.05 N ATOM 650 NH2 ARG A1085 31.482 27.415 27.593 1.00 43.73 N ATOM651 C ARG A1085 28.682 31.788 23.606 1.00 31.86 C ATOM 652 O ARG A108528.369 30.775 22.983 1.00 32.12 O ATOM 653 N GLY A1086 28.664 33.00623.070 1.00 30.59 N ATOM 654 CA GLY A1086 28.275 33.206 21.687 1.0029.15 C ATOM 655 C GLY A1086 26.779 33.208 21.427 1.00 28.22 C ATOM 656O GLY A1086 26.347 33.336 20.287 1.00 28.76 O ATOM 657 N ALA A108725.980 33.079 22.476 1.00 26.78 N ATOM 658 CA ALA A1087 24.536 33.05222.313 1.00 25.40 C ATOM 659 CB ALA A1087 23.907 32.162 23.378 1.0024.76 C ATOM 660 C ALA A1087 23.936 34.448 22.390 1.00 24.84 C ATOM 661O ALA A1087 24.417 35.304 23.142 1.00 24.29 O ATOM 662 N PRO A108822.886 34.703 21.591 1.00 23.94 N ATOM 663 CD PRO A1088 22.363 33.86420.496 1.00 23.58 C ATOM 664 CA PRO A1088 22.234 36.009 21.601 1.0023.19 C ATOM 665 CB PRO A1088 21.303 35.944 20.388 1.00 23.32 C ATOM 666CG PRO A1088 21.019 34.482 20.239 1.00 23.28 C ATOM 667 C PRO A108821.483 36.232 22.911 1.00 22.65 C ATOM 668 O PRO A1088 20.908 35.30423.475 1.00 22.59 O ATOM 669 N TYR A1089 21.518 37.464 23.407 1.00 22.22N ATOM 670 CA TYR A1089 20.824 37.808 24.645 1.00 21.73 C ATOM 671 CBTYR A1089 21.720 37.537 25.866 1.00 21.31 C ATOM 672 CG TYR A1089 22.84338.540 26.058 1.00 20.82 C ATOM 673 CD1 TYR A1089 22.795 39.475 27.0951.00 20.39 C ATOM 674 CE1 TYR A1089 23.791 40.428 27.253 1.00 20.46 CATOM 675 CD2 TYR A1089 23.931 38.582 25.177 1.00 20.50 C ATOM 676 CE2TYR A1089 24.942 39.535 25.323 1.00 20.31 C ATOM 677 CZ TYR A1089 24.86540.458 26.363 1.00 21.12 C ATOM 678 OH TYR A1089 25.844 41.421 26.5071.00 20.91 O ATOM 679 C TYR A1089 20.459 39.278 24.598 1.00 21.43 C ATOM680 O TYR A1089 20.986 40.045 23.782 1.00 21.20 O ATOM 681 N PHE A109019.541 39.670 25.469 1.00 21.81 N ATOM 682 CA PHE A1090 19.134 41.05825.534 1.00 21.85 C ATOM 683 CB PHE A1090 17.694 41.182 26.041 1.0020.99 C ATOM 684 CG PHE A1090 16.651 40.841 25.006 1.00 20.79 C ATOM 685CD1 PHE A1090 16.294 39.519 24.755 1.00 20.19 C ATOM 686 CD2 PHE A109016.052 41.849 24.247 1.00 20.29 C ATOM 687 CE1 PHE A1090 15.364 39.20723.760 1.00 19.79 C ATOM 688 CE2 PHE A1090 15.122 41.543 23.252 1.0020.00 C ATOM 689 CZ PHE A1090 14.778 40.221 23.007 1.00 19.21 C ATOM 690C PHE A1090 20.087 41.794 26.467 1.00 22.39 C ATOM 691 O PHE A109020.197 41.460 27.643 1.00 22.82 O ATOM 692 N SER A1091 20.791 42.78025.922 1.00 23.17 N ATOM 693 CA SER A1091 21.725 43.590 26.697 1.0024.38 C ATOM 694 CB SER A1091 22.879 44.048 25.805 1.00 24.43 C ATOM 695OG SER A1091 22.405 44.352 24.504 1.00 25.11 O ATOM 696 C SER A109120.979 44.805 27.248 1.00 24.91 C ATOM 697 O SER A1091 21.420 45.44328.204 1.00 24.93 O ATOM 698 N GLN A1092 19.854 45.124 26.618 1.00 25.07N ATOM 699 CA GLN A1092 19.023 46.235 27.046 1.00 26.14 C ATOM 700 CBGLN A1092 19.357 47.517 26.258 1.00 27.41 C ATOM 701 CG GLN A1092 20.77948.089 26.463 1.00 29.10 C ATOM 702 CD GLN A1092 21.096 48.475 27.9181.00 31.36 C ATOM 703 QE1 GLN A1092 20.273 49.093 28.607 1.00 32.18 OATOM 704 NE2 GLN A1092 22.306 48.127 28.380 1.00 31.33 N ATOM 705 C GLNA1092 17.556 45.850 26.841 1.00 25.78 C ATOM 706 O GLN A1092 17.14845.443 25.753 1.00 25.27 O ATOM 707 N ALA A1093 16.777 45.961 27.9091.00 25.60 N ATOM 708 CA ALA A1093 15.357 45.630 27.870 1.00 25.62 CATOM 709 CB ALA A1093 15.171 44.110 27.867 1.00 24.75 C ATOM 710 C ALAA1093 14.677 46.238 29.090 1.00 25.61 C ATOM 711 O ALA A1093 15.22046.209 30.186 1.00 25.48 O ATOM 712 N PRO A1094 13.474 46.796 28.9161.00 26.29 N ATOM 713 CD PRO A1094 12.668 46.878 27.682 1.00 26.31 CATOM 714 CA PRO A1094 12.758 47.400 30.046 1.00 26.85 C ATOM 715 CB PROA1094 11.622 48.147 29.358 1.00 26.71 C ATOM 716 CG PRO A1094 11.29247.223 28.222 1.00 26.01 C ATOM 717 C PRO A1094 12.241 46.343 31.0241.00 27.25 C ATOM 718 O PRO A1094 11.182 46.511 31.631 1.00 28.16 O ATOM719 N PHE A1095 12.980 45.248 31.167 1.00 26.92 N ATOM 720 CA PHE A109512.571 44.181 32.069 1.00 26.96 C ATOM 721 CB PHE A1095 12.234 42.91831.279 1.00 26.69 C ATOM 722 CG PHE A1095 11.729 41.782 32.127 1.0026.67 C ATOM 723 CD1 PHE A1095 12.396 40.553 32.137 1.00 26.30 C ATOM724 CD2 PHE A1095 10.567 41.920 32.879 1.00 25.87 C ATOM 725 CE1 PHEA1095 11.911 39.481 32.878 1.00 25.90 C ATOM 726 CE2 PHE A1095 10.07440.853 33.624 1.00 25.69 C ATOM 727 CZ PHE A1095 10.746 39.628 33.6251.00 26.13 C ATOM 728 C PHE A1095 13.685 43.891 33.055 1.00 26.99 C ATOM729 O PHE A1095 14.854 43.835 32.680 1.00 27.34 O ATOM 730 N SER A109613.319 43.687 34.314 1.00 26.53 N ATOM 731 CA SER A1096 14.308 43.43635.340 1.00 26.73 C ATOM 732 CB SER A1096 13.973 44.263 36.596 1.0027.70 C ATOM 733 OG SER A1096 12.642 44.023 37.052 1.00 29.18 O ATOM 734C SER A1096 14.500 41.968 35.715 1.00 26.21 C ATOM 735 O SER A109615.426 41.639 36.464 1.00 26.51 O ATOM 736 N GLY A1097 13.648 41.08835.198 1.00 25.26 N ATOM 737 CA GLY A1097 13.773 39.679 35.521 1.0024.11 C ATOM 738 C GLY A1097 14.633 38.918 34.529 1.00 24.17 C ATOM 739O GLY A1097 15.383 39.512 33.758 1.00 24.01 O ATOM 740 N LYS A109814.526 37.594 34.552 1.00 23.74 N ATOM 741 CA LYS A1098 15.281 36.74533.643 1.00 23.42 C ATOM 742 CB LYS A1098 15.360 35.309 34.172 1.0024.51 C ATOM 743 CG LYS A1098 16.177 35.141 35.444 1.00 26.65 C ATOM 744CD LYS A1098 16.236 33.682 35.898 1.00 28.23 C ATOM 745 CE LYS A109817.224 33.510 37.058 1.00 30.02 C ATOM 746 NZ LYS A1098 17.270 32.10837.594 1.00 30.95 N ATOM 747 C LYS A1098 14.602 36.730 32.287 1.00 22.48C ATOM 748 O LYS A1098 13.374 36.671 32.192 1.00 22.17 O ATOM 749 N ILEA1099 15.419 36.782 31.241 1.00 21.41 N ATOM 750 CA ILE A1099 14.94136.761 29.876 1.00 20.15 C ATOM 751 CB ILE A1099 15.333 38.039 29.1341.00 19.84 C ATOM 752 CG2 ILE A1099 14.804 37.989 27.713 1.00 20.13 CATOM 753 CG1 ILE A1099 14.791 39.263 29.873 1.00 19.76 C ATOM 754 CD1ILE A1099 15.218 40.583 29.262 1.00 18.64 C ATOM 755 C ILE A1099 15.57635.581 29.148 1.00 19.81 C ATOM 756 O ILE A1099 16.791 35.528 28.9721.00 20.43 O ATOM 757 N TRP A1100 14.761 34.623 28.740 1.00 19.20 N ATOM758 CA TRP A1100 15.277 33.480 28.005 1.00 18.42 C ATOM 759 CB TRP A110014.653 32.193 28.530 1.00 17.66 C ATOM 760 CG TRP A1100 14.970 31.96229.973 1.00 17.80 C ATOM 761 CD2 TRP A1100 16.150 31.351 30.501 1.0017.39 C ATOM 762 CE2 TRP A1100 16.038 31.375 31.914 1.00 17.58 C ATOM763 CE3 TRP A1100 17.294 30.787 29.921 1.00 17.40 C ATOM 764 CD1 TRPA1100 14.210 32.323 31.055 1.00 17.92 C ATOM 765 NE1 TRP A1100 14.84431.972 32.222 1.00 17.09 N ATOM 766 CZ2 TRP A1100 17.030 30.851 32.7591.00 16.77 C ATOM 767 CZ3 TRP A1100 18.283 30.268 30.763 1.00 17.50 CATOM 768 CH2 TRP A1100 18.138 30.307 32.167 1.00 17.07 C ATOM 769 C TRPA1100 14.946 33.700 26.526 1.00 17.86 C ATOM 770 O TRP A1100 13.79133.866 26.143 1.00 18.05 O ATOM 771 N LEU A1100 15.987 33.725 25.7071.00 17.46 N ATOM 772 CA LEU A1100 15.852 33.967 24.290 1.00 16.38 CATOM 773 CB LEU A1100 16.469 35.325 23.955 1.00 15.64 C ATOM 774 CG LEUA1100 16.715 35.601 22.468 1.00 15.15 C ATOM 775 CD1 LEU A1100 15.37935.873 21.762 1.00 13.79 C ATOM 776 CD2 LEU A1100 17.669 36.775 22.3171.00 14.27 C ATOM 777 C LEU A1100 16.520 32.916 23.429 1.00 16.47 C ATOM778 O LEU A1100 17.624 32.474 23.720 1.00 16.38 O ATOM 779 N SER A110215.847 32.520 22.356 1.00 17.12 N ATOM 780 CA SER A1102 16.429 31.56521.432 1.00 17.39 C ATOM 781 CB SER A1102 15.962 30.140 21.722 1.0016.65 C ATOM 782 OG SER A1102 16.736 29.217 20.966 1.00 15.28 O ATOM 783C SER A1102 16.052 31.965 20.011 1.00 18.55 C ATOM 784 O SER A110214.902 32.319 19.727 1.00 18.33 O ATOM 785 N ILE A1103 17.043 31.93019.127 1.00 19.20 N ATOM 786 CA ILE A1103 16.836 32.286 17.740 1.0020.42 C ATOM 787 CB ILE A1103 17.588 33.578 17.386 1.00 20.38 C ATOM 788CG2 ILE A1103 17.216 34.026 15.981 1.00 19.83 C ATOM 789 CG1 ILE A110317.240 34.675 18.399 1.00 20.72 C ATOM 790 CD1 ILE A1103 17.996 35.98018.172 1.00 20.84 C ATOM 791 C ILE A1103 17.347 31.169 16.843 1.00 21.44C ATOM 792 O ILE A1103 18.373 30.551 17.121 1.00 21.72 O ATOM 793 N SERA1104 16.625 30.916 15.764 1.00 21.94 N ATOM 794 CA SER A1104 17.01529.884 14.823 1.00 22.99 C ATOM 795 CB SER A1104 16.334 28.556 15.1851.00 22.73 C ATOM 796 OG SER A1104 16.618 27.550 14.229 1.00 21.97 OATOM 797 C SER A1104 16.607 30.322 13.421 1.00 23.89 C ATOM 798 O SERA1104 15.698 31.139 13.246 1.00 24.13 O ATOM 799 N HIS A1100 17.28329.787 12.417 1.00 25.15 N ATOM 800 CA HIS A1100 16.943 30.144 11.0491.00 26.29 C ATOM 801 CB HIS A1100 17.665 31.429 10.633 1.00 26.35 CATOM 802 CG HIS A1100 19.153 31.290 10.559 1.00 27.08 C ATOM 803 CD2 HISA1100 19.960 30.889 9.549 1.00 27.02 C ATOM 804 ND1 HIS A1100 19.98031.551 11.630 1.00 27.58 N ATOM 805 CE1 HIS A1100 21.234 31.317 11.2831.00 27.17 C ATOM 806 NE2 HIS A1100 21.249 30.914 10.025 1.00 27.22 NATOM 807 C HIS A1100 17.276 29.060 10.042 1.00 26.76 C ATOM 808 O HISA1100 18.031 28.129 10.318 1.00 26.55 O ATOM 809 N THR A1106 16.67029.197 8.874 1.00 27.49 N ATOM 810 CA THR A1106 16.901 28.309 7.751 1.0028.62 C ATOM 811 CB THR A1106 15.595 27.643 7.273 1.00 28.44 C ATOM 812OG1 THR A1106 14.721 28.635 6.712 1.00 27.15 O ATOM 813 CG2 THR A110614.901 26.954 8.447 1.00 28.62 C ATOM 814 C THR A1106 17.381 29.2996.698 1.00 29.33 C ATOM 815 O THR A1106 17.685 30.442 7.027 1.00 29.14 OATOM 816 N ASP A1107 17.446 28.880 5.444 1.00 30.59 N ATOM 817 CA ASPA1107 17.878 29.789 4.392 1.00 31.74 C ATOM 818 CB ASP A1107 18.32428.992 3.160 1.00 33.44 C ATOM 819 CG ASP A1107 19.499 28.054 3.454 1.0035.18 C ATOM 820 OD1 ASP A1107 19.827 27.214 2.582 1.00 36.15 O ATOM 821OD2 ASP A1107 20.099 28.153 4.548 1.00 35.79 O ATOM 822 C ASP A110716.720 30.722 4.020 1.00 31.63 C ATOM 823 O ASP A1107 16.913 31.7243.334 1.00 31.90 O ATOM 824 N GLN A1100 15.518 30.401 4.494 1.00 31.41 NATOM 825 CA GLN A1108 14.336 31.201 4.175 1.00 30.98 C ATOM 826 CB GLNA1108 13.340 30.345 3.399 1.00 32.64 C ATOM 827 CG GLN A1108 13.86029.898 2.038 1.00 34.63 C ATOM 828 CD GLN A1108 12.917 28.945 1.346 1.0035.98 C ATOM 829 OE1 GLN A1108 12.698 27.819 1.807 1.00 36.85 O ATOM 830NE2 GLN A1108 12.340 29.391 0.231 1.00 36.81 N ATOM 831 C GLN A110813.616 31.862 5.338 1.00 29.94 C ATOM 832 O GLN A1100 12.985 32.8995.158 1.00 29.44 O ATOM 833 N PHE A1109 13.700 31.269 6.529 1.00 29.06 NATOM 834 CA PHE A1109 13.024 31.838 7.692 1.00 27.73 C ATOM 835 CB PHEA1109 11.762 31.036 8.037 1.00 27.57 C ATOM 836 CG PHE A1109 10.74431.005 6.941 1.00 27.23 C ATOM 837 CD1 PHE A1109 10.788 30.017 5.9621.00 27.53 C ATOM 838 CD2 PHE A1109 9.749 31.976 6.871 1.00 27.16 C ATOM839 CE1 PHE A1109 9.852 30.000 4.921 1.00 27.28 C ATOM 840 CE2 PHE A11098.810 31.970 5.838 1.00 26.77 C ATOM 841 CZ PHE A1109 8.861 30.981 4.8611.00 26.97 C ATOM 842 C PHE A1109 13.868 31.932 8.950 1.00 26.95 C ATOM843 O PHE A1109 14.877 31.243 9.102 1.00 27.19 O ATOM 844 N VAL A111013.431 32.803 9.852 1.00 25.89 N ATOM 845 CA VAL A1110 14.080 32.99211.138 1.00 25.13 C ATOM 846 CB VAL A1110 14.844 34.347 11.197 1.0025.40 C ATOM 847 CG1 VAL A1110 13.874 35.510 11.081 1.00 25.64 C ATOM848 CG2 VAL A1110 15.623 34.449 12.499 1.00 25.77 C ATOM 849 C VAL A111012.956 32.973 12.184 1.00 24.39 C ATOM 850 O VAL A1110 11.863 33.50011.936 1.00 24.17 O ATOM 851 N THR A1111 13.206 32.344 13.332 1.00 23.30N ATOM 852 CA THR A1111 12.208 32.289 14.404 1.00 22.55 C ATOM 853 CBTHR A1111 11.610 30.888 14.562 1.00 22.93 C ATOM 854 OG1 THR A111112.670 29.954 14.786 1.00 24.79 O ATOM 855 CG2 THR A1111 10.839 30.47913.323 1.00 23.61 C ATOM 856 C THR A1111 12.830 32.664 15.746 1.00 21.62C ATOM 857 O THR A1111 13.999 32.377 16.002 1.00 21.64 O ATOM 858 N ALAA1112 12.041 33.299 16.605 1.00 20.37 N ATOM 859 CA ALA A1112 12.52233.688 17.922 1.00 19.66 C ATOM 860 CB ALA A1112 12.800 35.202 17.9701.00 19.55 C ATOM 861 C ALA A1112 11.516 33.311 19.004 1.00 19.07 C ATOM862 O ALA A1112 10.302 33.410 18.814 1.00 19.29 O ATOM 863 N SER A111312.034 32.872 20.139 1.00 17.99 N ATOM 864 CA SER A1113 11.195 32.50621.263 1.00 17.22 C ATOM 865 CB SER A1113 11.174 30;989 21.457 1.0016.88 C ATOM 866 OG SER A1113 10.313 30.614 22.521 1.00 16.26 O ATOM 867C SER A1113 11.782 33.180 22.487 1.00 17.09 C ATOM 868 O SER A111312.995 33.112 22.733 1.00 16.32 O ATOM 869 N VAL A1114 10.906 33.83123.245 1.00 17.10 N ATOM 870 CA VAL A1114 11.289 34.548 24.451 1.0016.74 C ATOM 871 CB VAL A1114 11.164 36.081 24.243 1.00 16.29 C ATOM 872CG1 VAL A1114 11.205 36.814 25.592 1.00 15.10 C ATOM 873 CG2 VAL A111412.298 36.574 23.329 1.00 16.31 C ATOM 874 C VAL A1114 10.422 34.14925.635 1.00 17.36 C ATOM 875 O VAL A1114 9.190 34.114 25.544 1.00 16.90O ATOM 876 N ILE A1115 11.073 33.834 26.747 1.00 17.78 N ATOM 877 CA ILEA1115 10.354 33.478 27.957 1.00 18.59 C ATOM 878 CB ILE A1115 10.63232.020 28.395 1.00 17.89 C ATOM 879 CG2 ILE A1115 9.806 31.691 29.6411.00 17.73 C ATOM 880 CG1 ILE A1115 10.247 31.053 27.272 1.00 18.13 CATOM 881 CD1 ILE A1115 10.654 29.599 27.521 1.00 17.22 C ATOM 882 C ILEA1115 10.830 34.431 29.049 1.00 19.32 C ATOM 883 O ILE A1115 12.02534.538 29.304 1.00 19.25 O ATOM 884 N LEU A1116 9.895 35.137 29.670 1.0020.62 N ATOM 885 CA LEU A1116 10.239 36.066 30.736 1.00 22.56 C ATOM 886CB LEU A1116 9.408 37.341 30.617 1.00 22.06 C ATOM 887 CG LEU A11169.547 38.064 29.272 1.00 22.11 C ATOM 888 CD1 LEU A1116 8.540 39.20729.187 1.00 21.22 C ATOM 889 CD2 LEU A1116 10.969 38.578 29.113 1.0021.72 C ATOM 890 C LEU A1116 9.984 35.379 32.069 1.00 24.06 C ATOM 891 OLEU A1116 8.936 34.765 32.275 1.00 23.78 O ATOM 892 N GLU A1117 10.95335.486 32.970 1.00 25.93 N ATOM 893 CA GLU A1117 10.857 34.843 34.2671.00 28.06 C ATOM 894 CB GLU A1117 11.604 33.502 34.204 1.00 28.05 CATOM 895 CG GLU A1117 11.800 32.793 35.536 1.00 28.32 C ATOM 896 CD GLUA1117 12.626 31.512 35.405 1.00 28.66 C ATOM 897 OE1 GLU A1117 13.71131.567 34.777 1.00 28.33 O ATOM 898 OE2 GLU A1117 12.196 30.458 35.9361.00 28.07 O ATOM 899 C GLU A1117 11.413 35.699 35.404 1.00 29.70 C ATOM900 O GLU A1117 12.242 36.583 35.190 1.00 29.81 O ATOM 901 N GLU A111810.928 35.441 36.615 1.00 31.64 N ATOM 902 CA GLU A1118 11.416 36.14137.794 1.00 33.73 C ATOM 903 CB GLU A1118 10.860 37.567 37.862 1.0035.16 C ATOM 904 CG GLU A1118 9.358 37.670 37.941 1.00 37.05 C ATOM 905CD GLU A1118 8.900 39.113 38.056 1.00 38.65 C ATOM 906 OE1 GLU A11189.476 39.973 37.348 1.00 38.82 O ATOM 907 OE2 GLU A1118 7.961 39.38538.848 1.00 39.77 O ATOM 908 C GLU A1118 11.043 35.365 39.048 1.00 34.16C ATOM 909 O GLU A1118 9.912 34.845 39.107 1.00 34.38 O ATOM 910 OXT GLUA1118 11.894 35.280 39.956 1.00 35.21 O TER 911 GLU A1118 ATOM 912 CBMET B2003 5.244 24.216 39.082 1.00 30.13 C ATOM 913 CG MET B2003 5.22922.763 38.655 1.00 32.03 C ATOM 914 SD MET B2003 4.499 21.640 39.8771.00 34.60 S ATOM 915 CE MET B2003 5.729 20.323 39.875 1.00 32.91 C ATOM916 C MET B2003 5.364 24.946 36.697 1.00 27.68 C ATOM 917 O MET B20034.190 25.254 36.454 1.00 27.76 O ATOM 918 N MET B2003 5.824 26.55538.533 1.00 28.66 N ATOM 919 CA MET B2003 5.954 25.143 38.090 1.00 28.51C ATOM 920 N ILE B2004 6.184 24.439 35.782 1.00 26.12 N ATOM 921 CA ILEB2004 5.730 24.192 34.423 1.00 24.36 C ATOM 922 CB ILE B2004 6.90724.200 33.423 1.00 23.97 C ATOM 923 CG2 ILE B2004 6.445 23.691 32.0621.00 22.87 C ATOM 924 CG1 ILE B2004 7.465 25.624 33.300 1.00 23.67 CATOM 925 CD1 ILE B2004 8.670 25.746 32.379 1.00 23.02 C ATOM 926 C ILEB2004 5.035 22.841 34.376 1.00 23.70 C ATOM 927 O ILE B2004 5.537 21.85434.917 1.00 23.27 O ATOM 928 N VAL B2005 3.866 22.793 33.748 1.00 22.71N ATOM 929 CA VAL B2005 3.151 21.530 33.660 1.00 22.27 C ATOM 930 CB VALB2005 1.853 21.564 34.494 1.00 21.83 C ATOM 931 CG1 VAL B2005 2.20421.793 35.959 1.00 21.47 C ATOM 932 CG2 VAL B2005 0.920 22.653 33.9941.00 21.79 C ATOM 933 C VAL B2005 2.847 21.133 32.228 1.00 22.00 C ATOM934 O VAL B2005 2.130 20.163 31.995 1.00 22.54 O ATOM 935 N GLY B20063.417 21.880 31.278 1.00 21.53 N ATOM 936 CA GLY B2006 3.225 21.59429.867 1.00 20.47 C ATOM 937 C GLY B2006 3.802 22.634 28.914 1.00 19.98C ATOM 938 O GLY B2006 3.873 23.820 29.237 1.00 20.12 O ATOM 939 N HISB2007 4.235 22.175 27.741 1.00 19.33 N ATOM 940 CA HIS B2007 4.78923.031 26.686 1.00 18.80 C ATOM 941 CB HIS B2007 6.301 23.191 26.8321.00 18.37 C ATOM 942 CG HIS B2007 6.945 23.945 25.708 1.00 18.59 C ATOM943 CD2 HIS B2007 8.088 23.712 25.015 1.00 19.30 C ATOM 944 ND1 HISB2007 6.447 25.138 25.226 1.00 18.65 N ATOM 945 CE1 HIS B2007 7.25425.607 24.289 1.00 18.01 C ATOM 946 NE2 HIS B2007 8.259 24.763 24.1431.00 18.26 N ATOM 947 C HIS B2007 4.482 22.387 25.342 1.00 18.69 C ATOM948 O HIS B2007 4.731 21.197 25.146 1.00 17.82 O ATOM 949 N GLY B20083.925 23.174 24.425 1.00 19.16 N ATOM 950 CA GLY B2008 3.599 22.65523.110 1.00 18.31 C ATOM 951 C GLY B2008 3.703 23.724 22.043 1.00 18.66C ATOM 952 O GLY B2008 3.378 24.890 22.297 1.00 18.62 O ATOM 953 N ILEB2009 4.175 23.336 20.858 1.00 18.12 N ATOM 954 CA ILE B2009 4.28224.257 19.736 1.00 18.56 C ATOM 955 CB ILE B2009 5.747 24.562 19.3511.00 18.23 C ATOM 956 CG2 ILE B2009 6.471 25.174 20.538 1.00 17.94 CATOM 957 CG1 ILE B2009 6.440 23.285 18.847 1.00 17.91 C ATOM 958 CD1 ILEB2009 7.819 23.525 18.220 1.00 16.62 C ATOM 959 C ILE B2009 3.601 23.65718.513 1.00 19.50 C ATOM 960 O ILE B2009 3.286 22.470 18.472 1.00 18.95O ATOM 961 N ASP B2010 3.356 24.492 17.518 1.00 20.39 N ATOM 962 CA ASPB2010 2.751 24.015 16.298 1.00 21.57 C ATOM 963 CB ASP B2010 1.25123.773 16.481 1.00 22.40 C ATOM 964 CG ASP B2010 0.635 22.980 15.3171.00 23.74 C ATOM 965 OD1 ASP B2010 0.223 23.595 14.308 1.00 23.88 OATOM 966 OD2 ASP B2010 0.576 21.731 15.415 1.00 24.74 O ATOM 967 C ASPB2010 2.979 25.019 15.200 1.00 22.11 C ATOM 968 O ASP B2010 3.032 26.22415.443 1.00 22.03 O ATOM 969 N ILE B2011 3.145 24.502 13.991 1.00 23.00N ATOM 970 CA ILE B2011 3.335 25.336 12.824 1.00 24.24 C ATOM 971 CB ILEB2011 4.818 25.320 12.339 1.00 24.43 C ATOM 972 CG2 ILE B2011 5.25823.905 11.972 1.00 24.62 C ATOM 973 CG1 ILE B2011 4.970 26.244 11.1331.00 25.18 C ATOM 974 CD1 ILE B2011 6.404 26.433 10.684 1.00 26.49 CATOM 975 C ILE B2011 2.398 24.818 11.732 1.00 25.03 C ATOM 976 O ILEB2011 2.257 23.609 11.532 1.00 24.85 O ATOM 977 N GLU B2011 1.733 25.74011.050 1.00 26.14 N ATOM 978 CA GLU B2011 0.813 25.377 9.979 1.00 27.22C ATOM 979 CB GLU B2011 0.636 25.692 10.369 1.00 28.06 C ATOM 980 CG GLUB2012 1.179 24.920 11.549 1.00 30.35 C ATOM 981 CD GLU B2011 1.23723.427 11.301 1.00 31.85 C ATOM 982 OE1 GLU B2011 1.472 23.026 10.1331.00 32.85 O ATOM 983 OE2 GLU B2011 1.065 22.660 12.278 1.00 31.85 OATOM 984 C GLU B2011 1.130 26.138 8.704 1.00 27.07 C ATOM 985 O GLUB2012 1.558 27.294 8.738 1.00 26.78 O ATOM 986 N GLU B2013 0.914 25.4717.579 1.00 27.58 N ATOM 987 CA GLU B2013 1.115 26.080 6.272 1.00 27.80 CATOM 988 CB GLU B2013 1.533 25.018 5.253 1.00 28.06 C ATOM 989 CG GLUB2013 1.806 25.553 3.851 1.00 29.06 C ATOM 990 CD GLU B2013 2.105 24.4472.858 0.05 28.78 C ATOM 991 OE1 GLU B2013 3.074 23.691 3.081 0.05 28.87O ATOM 992 OE2 GLU B2013 1.370 24.335 1.856 0.05 28.90 O ATOM 993 C GLUB2013 −0.268 26.626 5.939 1.00 27.67 C ATOM 994 O GLU B2013 −1.25025.894 5.982 1.00 27.29 O ATOM 995 N LEU B2014 −0.350 27.916 5.644 1.0028.07 N ATOM 996 CA LEU B2014 −1.629 28.542 5.330 1.00 28.65 C ATOM 997CB LEU B2014 −1.426 30.023 4.986 1.00 28.56 C ATOM 998 CG LEU B2014−1.332 31.022 6.147 1.00 28.97 C ATOM 999 CD1 LEU B2014 −2.677 31.1136.840 1.00 28.76 C ATOM 1000 CD2 LEU B2014 −0.260 30.593 7.139 1.0028.89 C ATOM 1001 C LEU B2014 −2.356 27.847 4.189 1.00 28.89 C ATOM 1002O LEU B2014 −3.584 27.758 4.189 1.00 28.92 O ATOM 1003 N ALA B2015−1.588 27.346 3.228 1.00 29.40 N ATOM 1004 CA ALA B2015 −2.137 26.6652.058 1.00 29.93 C ATOM 1005 CB ALA B2015 −0.999 26.206 1.146 1.00 29.23C ATOM 1006 C ALA B2015 −3.033 25.483 2.401 1.00 30.15 C ATOM 1007 O ALAB2015 −4.062 25.278 1.760 1.00 30.32 O ATOM 1008 N SER D2016 −2.64824.703 3.403 1.00 30.53 N ATOM 1009 CA SER B2016 −3.445 23.544 3.7761.00 31.47 C ATOM 1010 CB SER B2016 −2.625 22.583 4.640 1.00 31.89 CATOM 1011 OG SER B2016 −2.229 23.193 5.846 1.00 33.02 O ATOM 1012 C SERB2016 −4.735 23.946 4.487 1.00 31.84 C ATOM 1013 O SER B2016 −5.74123.243 4.391 1.00 31.71 O ATOM 1014 N ILE B2017 −4.716 25.068 5.201 1.0032.07 N ATOM 1015 CA ILE B2017 −5.932 25.527 5.861 1.00 32.52 C ATOM1016 CB ILE B2017 −5.651 26.688 6.843 1.00 32.37 C ATOM 1017 CG2 ILEB2017 −6.973 27.246 7.385 1.00 32.53 C ATOM 1018 CG1 ILE B2017 −4.75926.203 7.996 1.00 32.12 C ATOM 1019 CD1 ILE B2017 −5.399 25.165 8.8941.00 31.06 C ATOM 1020 C ILE B2017 −6.862 26.015 4.748 1.00 33.04 C ATOM1021 O ILE B2017 −8.084 25.862 4.821 1.00 32.69 O ATOM 1022 N GLU B2018−6.263 26.597 3.711 1.00 33.86 N ATOM 1023 CA GLU B2018 −7.006 27.0952.554 1.00 34.86 C ATOM 1024 CB GLU B2018 −6.042 27.669 1.504 1.00 36.31C ATOM 1025 CG GLU B2018 −5.544 29.080 1.764 1.00 38.14 C ATOM 1026 CDGLU B2018 −6.554 30.137 1.359 1.00 39.70 C ATOM 1027 OE1 GLU B2018−7.673 29.764 0.937 1.00 40.41 O ATOM 1028 OE2 GLU B2018 −6.231 31.3411.464 1.00 40.25 O ATOM 1029 C GLU B2018 −7.782 25.947 1.918 1.00 34.57C ATOM 1030 O GLU B2018 −8.964 26.076 1.612 1.00 34.08 O ATOM 1031 N SERB2019 −7.094 24.828 1.711 1.00 34.49 N ATOM 1032 CA SER B2019 −7.70523.650 1.103 1.00 34.60 C ATOM 1033 CB SER B2019 −6.639 22.610 0.7931.00 34.46 C ATOM 1034 OG SER B2019 −5.712 23.150 −0.125 1.00 35.85 OATOM 1035 C SER B2019 −8.761 23.039 1.996 1.00 34.54 C ATOM 1036 O SERB2019 −9.827 22.646 1.523 1.00 34.67 O ATOM 1037 N ALA B2020 −8.46322.965 3.290 1.00 34.29 N ATOM 1038 CA ALA B2020 −9.395 22.402 4.2511.00 34.25 C ATOM 1039 CB ALA B2020 −8.811 22.471 5.650 1.00 33.91 CATOM 1040 C ALA B2020 −10.703 23.175 4.180 1.00 34.65 C ATOM 1041 O ALAB2020 −11.778 22.579 4.133 1.00 34.60 O ATOM 1042 N VAL B2021 −10.60424.502 4.151 1.00 35.08 N ATOM 1043 CA VAL B2021 −11.784 25.359 4.0731.00 35.39 C ATOM 1044 CB VAL B2021 −11.411 26.855 4.220 1.00 35.27 CATOM 1045 CG1 VAL B2021 −12.608 27.732 3.884 1.00 34.79 C ATOM 1046 CG2VAL B2021 −10.951 27.136 5.637 1.00 35.33 C ATOM 1047 C VAL B2021−12.526 25.174 2.756 1.00 36.00 C ATOM 1048 O VAL B2021 −13.746 24.9852.749 1.00 35.93 O ATOM 1049 N THR B2022 −11.795 25.237 1.644 1.00 36.68N ATOM 1050 CA THR B2022 −12.401 25.072 0.326 1.00 37.80 C ATOM 1051 CBTHR B2022 −11.351 25.211 −0.813 1.00 38.05 C ATOM 1052 OG1 THR B2022−10.830 26.549 −0.839 1.00 37.71 O ATOM 1053 CG2 THR B2022 −11.98824.898 −2.166 1.00 37.87 C ATOM 1054 C THR B2022 −13.064 23.701 0.2101.00 38.58 C ATOM 1055 O THR B2022 −14.204 23.584 −0.234 1.00 38.63 OATOM 1056 N ARG B2023 −12.348 22.666 0.629 1.00 39.65 N ATOM 1057 CA ARGB2023 −12.864 21.306 0.563 1.00 41.03 C ATOM 1058 CB ARG B2023 −11.82820.317 1.106 1.00 41.66 C ATOM 1059 CG ARG B2023 −11.891 18.939 0.4521.00 43.04 C ATOM 1060 CD ARG B2023 −13.312 18.416 0.395 1.00 43.90 CATOM 1061 NE ARG B2023 −13.406 17.090 −0.202 1.00 44.75 N ATOM 1062 CZARG B2023 −14.524 16.371 −0.231 1.00 45.34 C ATOM 1063 NH1 ARG B2023−15.638 16.862 0.302 1.00 45.03 N ATOM 1064 NH2 ARG B2023 −14.527 15.157−0.773 1.00 45.61 N ATOM 1065 C ARG B2023 −14.165 21.138 1.343 1.0041.52 C ATOM 1066 O ARG B2023 −15.180 20.712 0.787 1.00 41.49 O ATOM1067 N HIS B2024 −14.120 21.467 2.631 1.00 41.94 N ATOM 1068 CA HISB2024 −15.274 21.343 3.511 1.00 42.45 C ATOM 1069 CB HIS B2024 −14.93120.424 4.678 1.00 43.39 C ATOM 1070 CG HIS B2024 −14.516 19.050 4.2551.00 44.50 C ATOM 1071 CD2 HIS B2024 −13.294 18.468 4.191 1.00 44.72 CATOM 1072 ND1 HIS B2024 −15.411 18.115 3.777 1.00 45.05 N ATOM 1073 CE1HIS B2024 −14.758 17.018 3.436 1.00 45.22 C ATOM 1074 NE2 HIS B2024−13.473 17.206 3.677 1.00 45.24 N ATOM 1075 C HIS B2024 −15.713 22.6974.040 1.00 42.58 C ATOM 1076 O HIS B2024 −14.934 23.412 4.672 1.00 42.87O ATOM 1077 N GLU B2025 −16.967 23.050 3.781 1.00 42.39 N ATOM 1078 CAGLU B2025 −17.490 24.326 4.242 1.00 41.91 C ATOM 1079 CB GLU B2025−18.732 24.732 3.437 1.00 43.59 C ATOM 1080 CG GLU B2025 −18.797 26.2293.153 1.00 45.80 C ATOM 1081 CD GLU B2025 −20.117 26.675 2.544 1.0047.26 C ATOM 1082 OE1 GLU B2025 −20.610 26.003 1.603 1.00 47.52 O ATOM1083 OE2 GLU B2025 −20.653 27.710 3.006 1.00 48.07 O ATOM 1084 C GLUB2025 −17.848 24.211 5.712 1.00 40.39 C ATOM 1085 O GLU B2025 −18.17225.203 6.356 1.00 40.62 O ATOM 1086 N GLY B2026 −17.789 22.993 6.2381.00 38.87 N ATOM 1087 CA GLY B2026 −18.105 22.788 7.638 1.00 36.84 CATOM 1088 C GLY B2026 −16.865 22.836 8.507 1.00 35.50 C ATOM 1089 O GLYB2026 −16.954 22.961 9.732 1.00 35.89 O ATOM 1090 N PHE B2027 −15.70622.746 7.866 1.00 33.86 N ATOM 1091 CA PHE B2027 −14.416 22.752 8.5491.00 32.08 C ATOM 1092 CB PHE B2027 −13.293 22.958 7.532 1.00 31.28 CATOM 1093 CG PHE B2027 −11.926 22.896 8.128 1.00 29.92 C ATOM 1094 CD1PHE B2027 −11.396 21.682 8.555 1.00 28.97 C ATOM 1095 CD2 PHE B2027−11.176 24.054 8.293 1.00 29.17 C ATOM 1096 CE1 PHE B2027 −10.143 21.6239.135 1.00 28.66 C ATOM 1097 CE2 PHE B2027 −9.918 24.006 8.875 1.0028.77 C ATOM 1098 CZ PHE B2027 −9.399 22.790 9.298 1.00 28.68 C ATOM1099 C PHE B2027 −14.294 23.801 9.651 1.00 31.46 C ATOM 1100 O PHE B2027−14.059 23.465 10.815 1.00 31.23 O ATOM 1101 N ALA B2028 −14.454 25.0679.278 1.00 30.51 N ATOM 1102 CA ALA B2028 −14.360 26.169 10.228 1.0030.25 C ATOM 1103 CB ALA B2028 −14.624 27.487 9.517 1.00 30.53 C ATOM1104 C ALA B2028 −15.305 26.030 11.421 1.00 30.13 C ATOM 1105 O ALAB2028 −14.926 26.308 12.561 1.00 29.80 O ATOM 1106 N LYS B2029 −16.53325.600 11.160 1.00 30.02 N ATOM 1107 CA LYS B2029 −17.520 25.448 12.2251.00 30.10 C ATOM 1108 CB LYS B2029 −18.882 25.053 11.637 1.00 30.49 CATOM 1109 CG LYS B2029 −19.552 26.148 10.821 1.00 31.20 C ATOM 1110 CDLYS B2029 −20.765 25.618 10.074 0.05 30.87 C ATOM 1111 CE LYS B2029−21.354 26.675 9.153 0.05 30.89 C ATOM 1112 NZ LYS B2029 −22.504 26.1508.365 0.05 30.76 N ATOM 1113 C LYS B2029 −17.099 24.408 13.248 1.0029.50 C ATOM 1114 O LYS B2029 −17.467 24.491 14.420 1.00 29.99 O ATOM1115 N ARG B2030 −16.326 23.428 12.798 1.00 28.70 N ATOM 1116 CA ARGB2030 −15.877 22.348 13.667 1.00 27.83 C ATOM 1117 CB ARG B2030 −15.61621.093 12.822 1.00 27.88 C ATOM 1118 CG ARG B2030 −16.867 20.503 12.1930.05 27.87 C ATOM 1119 CD ARG B2030 −16.543 19.293 11.332 0.05 27.87 CATOM 1120 NE ARG B2030 −15.748 19.648 10.160 0.05 27.89 N ATOM 1121 CZARG B2030 −15.379 18.785 9.218 0.05 27.88 C ATOM 1122 NH1 ARG B2030−15.732 17.510 9.309 0.05 27.89 N ATOM 1123 NH2 ARG B2030 −14.658 19.1968.184 0.05 27.87 N ATOM 1124 C ARG B2030 −14.631 22.698 14.477 1.0026.83 C ATOM 1125 O ARG B2030 −14.391 22.134 15.541 1.00 26.57 O ATOM1126 N VAL B2031 −13.854 23.644 13.965 1.00 25.79 N ATOM 1127 CA VALB2031 −12.610 24.073 14.596 1.00 24.76 C ATOM 1128 CB VAL B2031 −11.56524.442 13.505 1.00 24.82 C ATOM 1129 CG1 VAL B2031 −10.365 25.139 14.1211.00 24.72 C ATOM 1130 CG2 VAL B2031 −11.125 23.184 12.779 1.00 24.93 CATOM 1131 C VAL B2031 −12.806 25.263 15.523 1.00 23.81 C ATOM 1132 O VALB2031 −12.166 25.365 16.568 1.00 22.82 O ATOM 1133 N LEU B2032 −13.70926.149 15.127 1.00 23.54 N ATOM 1134 CA LEU B2032 −13.997 27.361 15.8731.00 23.22 C ATOM 1135 CB LEU B2032 −14.157 28.528 14.893 1.00 22.85 CATOM 1136 CG LEU B2032 −12.924 28.789 14.022 1.00 22.24 C ATOM 1137 CD1LEU B2032 −13.210 29.906 13.026 1.00 22.1.1 C ATOM 1138 CD2 LEU B2032−11.747 29.152 14.918 1.00 22.17 C ATOM 1139 C LEU B2032 −15.233 27.25616.744 1.00 23.32 C ATOM 1140 O LEU B2032 −16.122 26.454 16.482 1.0023.42 O ATOM 1141 N THR B2033 −15.263 28.060 17.803 1.00 23.69 N ATOM1142 CA THR B2033 −16.404 28.105 18.713 1.00 23.81 C ATOM 1143 CB THRB2033 −16.002 28.538 20.129 1.00 23.49 C ATOM 1144 OG1 THR B2033 −15.44229.858 20.074 1.00 23.22 O ATOM 1145 CG2 THR B2033 −15.004 27.571 20.7261.00 22.82 C ATOM 1146 C THR B2033 −17.312 29.191 18.162 1.00 24.17 CATOM 1147 O THR B2033 −16.915 29.930 17.264 1.00 24.05 O ATOM 1148 N ALAB2034 −18.516 29.302 18.709 1.00 24.73 N ATOM 1149 CA ALA B2034 −19.45630.322 18.246 1.00 25.88 C ATOM 1150 CB ALA B2034 −20.704 30.326 19.1271.00 25.52 C ATOM 1151 C ALA B2034 −18.793 31.704 18.245 1.00 26.34 CATOM 1152 O ALA B2034 −18.815 32.409 17.231 1.00 26.66 O ATOM 1153 N LEUB2035 −18.194 32.083 19.374 1.00 27.02 N ATOM 1154 CA LEU B2035 −17.51833.375 19.477 1.00 27.85 C ATOM 1155 CB LEU B2035 −16.868 33.549 20.8521.00 28.57 C ATOM 1156 CG LEU B2035 −17.760 33.942 22.028 1.00 29.51 CATOM 1157 CD1 LEU B2035 −16.879 34.241 23.246 1.00 29.47 C ATOM 1158 CD2LEU B2035 −18.596 35.181 21.648 1.00 29.85 C ATOM 1159 C LEU B2035−16.445 33.516 18.405 1.00 28.07 C ATOM 1160 O LEU B2035 −16.395 34.51611.687 1.00 28.48 O ATOM 1161 N GLU B2036 −15.578 32.518 18.308 1.0027.90 N ATOM 1162 CA GLU B2036 −14.518 32.542 17.310 1.00 27.73 C ATOM1163 CB GLU B2036 −13.666 31.270 17.414 1.00 26.50 C ATOM 1164 CG GLUB2036 −12.568 31.339 18.474 1.00 25.25 C ATOM 1165 CD GLU B2036 −11.96929.976 18.799 1.00 24.47 C ATOM 1166 OE1 GLU B2036 −10.797 29.925 19.2261.00 23.46 O ATOM 1167 OE2 GLU B2036 −12.676 28.957 18.636 1.00 24.23 OATOM 1166 C GLU B2036 −15.073 32.686 15.895 1.00 28.15 C ATOM 1169 O GLUB2036 −14.507 33.403 15.083 1.00 28.18 O ATOM 1170 N MET B2037 −16.16931.990 15.604 1.00 29.30 N ATOM 1171 CA MET B2037 −16.800 32.038 14.2831.00 30.55 C ATOM 1172 CB MET B2037 −17.984 31.069 14.211 1.00 30.95 CATOM 1173 CG MET B2037 −17.607 29.662 13.809 1.00 31.93 C ATOM 1174 SDMET B2037 −16.851 29.650 12.173 1.00 33.36 S ATOM 1175 CE MET B2037−18.331 29.638 11.166 1.00 32.65 C ATOM 1176 C MET B2037 −17.286 33.43613.934 1.00 31.15 C ATOM 1177 O MET B2037 −17.206 33.854 12.785 1.0030.76 O ATOM 1178 N GLU B2038 −17.789 34.153 14.934 1.00 32.42 N ATOM1179 CA GLU B2038 −18.278 35.513 14.730 1.00 33.88 C ATOM 1180 CB GLUB2038 −18.841 36.062 16.044 1.00 35.07 C ATOM 1181 CG GLU B2038 −19.43237.455 15.931 1.00 37.91 C ATOM 1182 CD GLU B2038 −20.528 37.714 16.9551.00 39.72 C ATOM 1183 OE1 GLU B2038 −21.587 37.050 16.864 1.00 40.71 OATOM 1184 OE2 GLU B2038 −20.333 38.576 17.846 1.00 40.42 O ATOM 1185 CGLU B2038 −17.163 36.418 14.198 1.00 34.07 C ATOM 1186 O GLU B2038−17.406 37.320 13.397 1.00 33.98 O ATOM 1187 N ARG B2039 −15.936 36.18114.649 1.00 34.44 N ATOM 1188 CA ARG B2039 −14.810 36.972 14.179 1.0035.18 C ATOM 1189 CB ARG B2039 −13.630 36.856 15.153 1.00 35.30 C ATOM1190 CG ARG B2039 −12.370 37.601 14.720 1.00 35.26 C ATOM 1191 CD ARGB2039 −12.590 39.099 14.608 0.05 35.23 C ATOM 1192 NE ARG B2039 −11.35839.788 14.235 0.05 35.24 N ATOM 1193 CZ ARG B2039 −11.260 41.099 14.0400.05 35.24 C ATOM 1194 NH1 ARG B2039 −10.095 41.634 13.703 0.05 35.27 NATOM 1195 NH2 ARG B2039 −12.325 41.875 14.182 0.05 35.27 N ATOM 1196 CARG B2039 −14.418 36.445 12.797 1.00 35.34 C ATOM 1197 O ARG B2039−14.167 37.217 11.868 1.00 35.66 O ATOM 1198 N PHE B2040 −14.382 35.12312.673 1.00 35.29 N ATOM 1199 CA PHE B2040 −14.042 34.473 11.414 1.0035.77 C ATOM 1200 CB PHE B2040 −14.241 32.961 11.545 1.00 34.55 C ATOM1201 CG PHE B2040 −13.996 32.201 10.271 1.00 33.98 C ATOM 1202 CD1 PHEB2040 −12.716 32.122 9.725 1.00 33.52 C ATOM 1203 CD2 PHE B2040 −15.04531.564 9.614 1.00 33.68 C ATOM 1204 CE1 PHE B2040 −12.488 31.420 8.5481.00 33.41 C ATOM 1205 CE2 PHE B2040 −14.828 30.861 8.435 1.00 33.27 CATOM 1206 CZ PHE B2040 −13.549 30.787 7.899 1.00 33.46 C ATOM 1207 C PHEB2040 −14.916 34.997 10.268 1.00 36.68 C ATOM 1208 O PHE B2040 −14.44535.199 9.144 1.00 36.38 O ATOM 1209 N THR B2041 −16.191 35.221 10.5611.00 37.87 N ATOM 1210 CA THR B2041 −17.121 35.692 9.546 1.00 39.25 CATOM 1211 CB THR B2041 −18.580 35.450 9.981 1.00 39.24 C ATOM 1212 OG1THR B2041 −18.811 34.041 10.115 1.00 39.45 O ATOM 1213 CG2 THR B2041−19.540 36.001 8.943 1.00 40.16 C ATOM 1214 C THR B2041 −16.947 37.1599.159 1.00 39.72 C ATOM 1215 O THR B2041 −17.496 37.598 8.157 1.00 40.46O ATOM 1216 N SER B2042 −16.175 37.915 9.930 1.00 40.14 N ATOM 1217 CASER B2042 −15.970 39.327 9.609 1.00 40.54 C ATOM 1218 CB SER B2042−16.159 40.184 10.8S8 1.00 40.81 C ATOM 1219 OG SER B2042 −17.449 39.98911.399 1.00 42.55 O ATOM 1220 C SER B2O42 −14.588 39.596 9.033 1.0040.43 C ATOM 1221 O SER B2042 −14.039 40.686 9.218 1.00 40.73 O ATOM1222 N LEU B2043 −14.031 38.615 6.327 1.00 39.91 N ATOM 1223 CA LEUB2043 −12.698 38.764 7.758 1.00 39.34 C ATOM 1224 CB LEU B2043 −11.66338.115 8.683 1.00 38.78 C ATOM 1225 CG LEU B2043 −11.484 38.654 10.1051.00 38.39 C ATOM 1226 CD1 LEU B2043 −10.642 37.666 10.913 1.00 37.70 CATOM 1227 CD2 LEU B2043 −10.822 40.035 10.075 1.00 37.83 C ATOM 1228 CLEU B2043 −12.555 38.165 6.360 1.00 39.45 C ATOM 1229 O LEU B2043−11.502 38.317 5.732 1.00 39.47 O ATOM 1230 N LYS B2044 −13.594 37.4785.884 1.00 38.98 N ATOM 1231 CA LYS B2044 −13.569 36.850 4.556 1.0038.77 C ATOM 1232 CB LYS B2044 −14.875 37.145 3.807 1.00 39.18 C ATOM1233 CG LYS B2044 −14.988 36.486 2.442 0.05 38.97 C ATOM 1234 CD LYSB2044 −15.072 34.973 2.556 0.05 38.99 C ATOM 1235 CE LYS B2044 −15.26334.332 1.191 0.05 38.96 C ATOM 1236 NZ LYS B2044 −15.382 32.851 1.2840.05 38.96 N ATOM 1237 C LYS B2044 −12.383 37.340 3.720 1.00 38.31 CATOM 1238 O LYS B2044 −12.253 38.538 3.458 1.00 38.14 O ATOM 1239 N GLYB2045 −11.522 36.412 3.310 1.00 37.92 N ATOM 1240 CA GLY B2045 −10.35136.767 2.521 1.00 36.95 C ATOM 1241 C GLY B2045 −9.108 36.124 3.108 1.0036.64 C ATOM 1242 O GLY B2045 −9.207 35.141 3.845 1.00 37.08 O ATOM 1243N ARG B2046 −7.935 36.665 2.607 1.00 35.68 N ATOM 1244 CA ARG B2046−6.703 36.084 3.332 1.00 35.35 C ATOM 1245 CB ARG B2046 −5.476 36.8042.750 1.00 35.15 C ATOM 1246 CG ARG B2046 −4.150 36.148 3.087 0.05 35.14C ATOM 1247 CD ARG B2046 −4.081 34.743 2.515 0.05 35.11 C ATOM 1248 NEARG B2046 −2.811 34.090 2.811 0.05 35.11 N ATOM 1249 CZ ARG B2046 −2.50432.853 2.436 0.05 35.09 C ATOM 1250 NH1 ARG B2046 −1.323 32.338 2.7480.05 35.09 N ATOM 1251 NH2 ARG B2046 −3.377 32.130 1.748 0.05 35.07 NATOM 1252 C ARG B2046 −6.661 36.147 4.859 1.00 34.86 C ATOM 1253 O ARGB2046 −6.273 35.184 5.522 1.00 34.07 O ATOM 1254 N ARG B2047 −7.06837.289 5.407 1.00 34.76 N ATOM 1255 CA ARG B2047 −7.074 37.503 6.8521.00 35.00 C ATOM 1256 CB ARG B2047 −7.559 38.918 7.156 1.00 35.75 CATOM 1257 CG ARG B2047 −6.762 39.984 6.434 1.00 37.57 C ATOM 1258 CD ARGB2047 −7.345 41.342 6.697 1.00 39.01 C ATOM 1259 NE ARG B2047 −8.74341.398 6.289 1.00 40.76 N ATOM 1260 CZ ARG B2047 −9.663 42.124 6.9151.00 41.64 C ATOM 1261 NH1 ARG B2047 −9.322 42.852 7.974 1.00 41.91 NATOM 1262 NH2 ARG B2047 −10.924 42.110 6.497 1.00 42.15 N ATOM 1263 CARG B2047 −7.959 36.483 7.566 1.00 34.24 C ATOM 1264 O ARG B2047 −7.68136;070 8.692 1.00 34.10 O ATOM 1265 N GLN B2048 −9.030 36.085 6.900 1.0033.32 N ATOM 1266 CA GLN B2048 −9.944 35.112 7.460 1.00 32.27 C ATOM1267 CB GLN B2048 −11.138 34.961 6.531 1.00 32.92 C ATOM 1268 CG GLNB2048 −12.281 34.193 7.115 1.00 33.21 C ATOM 1269 CD GLN B2048 −13.32333.871 6.077 1.00 33.65 C ATOM 1270 OE1 GLN B2048 −13.016 33.274 5.0441.00 34.07 O ATOM 1271 NE2 GLN B2048 −14.567 34.258 6.343 1.00 33.98 NATOM 1272 C GLN B2048 −9.224 33.772 7.620 1.00 31.20 C ATOM 1273 O GLNB2048 −9.402 33.075 8.615 1.00 30.73 O ATOM 1274 N ILE B2049 −8.40533.419 6.634 1.00 29.96 N ATOM 1275 CA ILE B2049 −7.661 32.170 6.6821.00 28.94 C ATOM 1276 CB ILE B2049 −7.007 31.856 5.313 1.00 28.51 CATOM 1277 CG2 ILE B2049 −6.069 30.658 5.438 1.00 27.59 C ATOM 1278 CG1ILE B2049 −8.096 31.573 4.267 1.00 28.47 C ATOM 1279 CD1 ILE B2049−8.950 30.333 4.553 1.00 27.80 C ATOM 1280 C ILE B2049 −6.574 32.1987.759 1.00 28.73 C ATOM 1281 O ILE B2049 −6.353 31.206 8.463 1.00 28.34O ATOM 1282 N GLU B2050 −5.896 33.336 7.879 1.00 28.38 N ATOM 1283 CAGLU B2050 −4.833 33.494 8.859 1.00 28.07 C ATOM 1284 CB GLU B2050 −4.15134.848 8.665 1.00 29.65 C ATOM 1285 CG GLU B2050 −3.799 35.103 7.2001.00 32.92 C ATOM 1286 CD GLU B2050 −2.865 36.279 6.995 1.00 34.62 CATOM 1287 OE1 GLU B2050 −3.232 37.416 7.392 1.00 35.24 O ATOM 1288 OE2GLU B2050 −1.762 36.055 6.430 1.00 35.19 O ATOM 1289 C GLU B2050 −5.41633.374 10.260 1.00 26.78 C ATOM 1290 O GLU B2050 −4.812 32.768 11.1501.00 26.09 O ATOM 1291 N TYR B2051 −6.600 33.944 10.453 1.00 25.41 NATOM 1292 CA TYR B2051 −7.251 33.868 11.749 1.00 24.34 C ATOM 1293 CBTYR B2051 −8.535 34.703 11.741 1.00 23.37 C ATOM 1294 CG TYR B2051−9.316 34.618 13.024 1.00 22.77 C ATOM 1295 CD1 TYR B2051 −10.347 33.69513.169 1.00 22.86 C ATOM 1296 CE1 TYR B2051 −11.026 33.559 14.369 1.0023.29 C ATOM 1297 CD2 TYR B2051 −8.984 35.413 14.116 1.00 22.81 C ATOM1298 CE2 TYR B2051 −9.657 35.284 15.332 1.00 23.14 C ATOM 1299 CZ TYRB2051 −10.677 34.350 15.450 1.00 23.43 C ATOM 1300 OH TYR B2051 −11.33234.186 16.649 1.00 23.03 O ATOM 1301 C TYR B2051 −7.550 32.400 12.0861.00 24.05 C ATOM 1302 O TYR B2051 −7.176 31.910 13.154 1.00 24.52 OATOM 1303 N LEU B2052 −8.211 31.700 11.170 1.00 23.25 N ATOM 1304 CA LEUB2052 −8.541 30.291 11.364 1.00 22.91 C ATOM 1305 CB LEU B2052 −9.27429.748 10.133 1.00 22.55 C ATOM 1306 CG LEU B2052 −9.598 28.247 10.0861.00 22.85 C ATOM 1307 CD1 LEU B2052 −10.345 27.814 11.343 1.00 21.95 CATOM 1308 CD2 LEU B2052 −10.436 27.957 8.835 1.00 22.89 C ATOM 1309 CLEU B2052 −7.284 29.457 11.622 1.00 22.68 C ATOM 1310 O LEU B2052 −7.23228.681 12.571 1.00 22.94 O ATOM 1311 N ALA B2053 −6.285 29.612 10.7611.00 22.31 N ATOM 1312 CA ALA B2053 −5.024 28.897 10.884 1.00 21.99 CATOM 1313 CB ALA B2053 −4.072 29.332 9.774 1.00 21.32 C ATOM 1314 C ALAB2053 −4.397 29.180 12.244 1.00 22.13 C ATOM 1315 O ALA B2053 −3.80528.295 12.868 1.00 21.87 O ATOM 1316 N GLY B2054 −4.532 30.427 12.6881.00 21.95 N ATOM 1317 CA GLY B2054 −3.981 30.829 13.963 1.00 21.46 CATOM 1318 C GLY B2054 −4.654 30.111 15.107 1.00 21.35 C ATOM 1319 O GLYB2054 −3.986 29.678 16.049 1.00 21.19 O ATOM 1320 N ARG B2055 −5.91429.976 15.040 1.00 20.89 N ATOM 1321 CA ARG B2055 −6.681 29.290 16.1141.00 20.89 C ATOM 1322 CB ARG B2055 −8.191 29.543 16.034 1.00 20.27 CATOM 1323 CG ARG B2055 −8.685 30.688 16.934 1.00 19.89 C ATOM 1324 CDARG B2055 −7.926 31.986 16.664 1.00 20.08 C ATOM 1325 NE ARG B2055−8.265 33.046 17.609 1.00 19.79 N ATOM 1326 CZ ARG B2055 −7.634 34.21617.668 1.00 20.91 C ATOM 1327 NH1 ARG B2055 −6.626 34.473 16.832 1.0020.64 N ATOM 1328 NH2 ARG B2055 −8.009 35.135 18.555 1.00 20.13 N ATOM1329 C ARG B2055 −6.383 27.796 16.086 1.00 20.73 C ATOM 1330 O ARG B2055−6.239 27.169 17.136 1.00 20.29 O ATOM 1331 N TRP B2056 −6.273 27.23514.884 1.00 20.69 N ATOM 1332 CA TRP B2056 −5.976 25.817 14.742 1.0020.72 C ATOM 1333 CB TRP B2056 −5.992 25.408 13.262 1.00 21.90 C ATOM1334 CG TRP B2056 −5.402 24.051 13.020 1.00 23.77 C ATOM 1335 CD2 TRPB2056 −6.116 22.814 12.903 1.00 24.30 C ATOM 1336 CE2 TRP B2056 −5.15121.780 12.814 1.00 24.91 C ATOM 1337 CE3 TRP B2056 −7.473 22.478 12.8691.00 24.91 C ATOM 1338 CD1 TRP B2056 −4.065 23.727 12.983 1.00 23.97 CATOM 1339 NE1 TRP B2056 −3.912 22.365 12.864 1.00 24.86 N ATOM 1340 CZ2TRP B2056 −5.505 20.429 12.697 1.00 25.50 C ATOM 1341 CZ3 TRP B2056−7.829 21.131 12.751 1.00 26.26 C ATOM 1342 CH2 TRP B2056 −6.843 20.12212.667 1.00 26.22 C ATOM 1343 C TRP B2056 −4.603 25.547 15.348 1.0020.41 C ATOM 1344 O TRP B2056 −4.409 24.582 16.093 1.00 20.04 O ATOM1345 N SER B2057 −3.654 26.415 15.025 1.00 19.64 N ATOM 1346 CA SERB2057 −2.298 26.282 15.533 1.00 19.83 C ATOM 1347 CB SER B2057 −1.39527.339 14.898 1.00 20.26 C ATOM 1348 OG SER B2057 −0.057 27.136 15.3031.00 22.97 O ATOM 1349 C SER B2057 −2.239 26.402 17.062 1.00 18.86 CATOM 1350 O SER B2057 −1.548 25.636 17.725 1.00 18.27 O ATOM 1351 N ALAB2058 −2.968 27.367 17.613 1.00 18.16 N ATOM 1352 CA ALA B2058 −2.99627.566 19.058 1.00 17.01 C ATOM 1353 CB ALA B2058 −3.767 28.826 19.3881.00 16.89 C ATOM 1354 C ALA B2058 −3.623 26.365 19.781 1.00 16.76 CATOM 1355 O ALA B2058 −3.087 25.890 20.783 1.00 15.81 O ATOM 1356 N LYSB2059 −4.755 25.884 19.272 1.00 16.40 N ATOM 1357 CA LYS B2059 −5.44624.746 19.883 1.00 17.29 C ATOM 1358 CB LYS B2059 −6.815 24.547 19.2171.00 16.13 C ATOM 1359 CG LYS B2059 −7.751 25.730 19.498 1.00 15.32 CATOM 1360 CD LYS B2059 −9.168 25.536 18.996 1.00 14.90 C ATOM 1361 CELYS B2059 −10.011 26.783 19.319 1.00 13.82 C ATOM 1362 NZ LYS B2059−11.432 26.637 18.937 1.00 11.65 N ATOM 1363 C LYS B2059 −4.620 23.46419.826 1.00 17.91 C ATOM 1364 O LYS B2059 −4.640 22.656 20.748 1.0016.96 O ATOM 1365 N GLU B2060 −3.879 23.293 18.738 1.00 19.43 N ATOM1366 CA GLU B2060 −3.043 22.123 18.585 1.00 20.86 C ATOM 1367 CB GLUB2060 −2.516 22.046 17.146 1.00 22.77 C ATOM 1368 CG GLU B2060 −1.96420.691 16.759 1.00 26.37 C ATOM 1369 CD GLU B2060 −2.982 19.574 16.9591.00 29.21 C ATOM 1370 OE1 GLU B2060 −4.047 19.602 16.287 1.00 29.92 OATOM 1371 OE2 GLU B2060 −2.720 18.670 17.795 1.00 30.31 O ATOM 1372 CGLU B2060 −1.889 22.256 19.593 1.00 20.86 C ATOM 1373 O GLU B2060 −1.55621.302 20.307 1.00 20.96 O ATOM 1374 N ALA B2061 −1.299 23.447 19.6611.00 20.25 N ATOM 1375 CA ALA B2061 −0.191 23,697 20.580 1.00 20.38 CATOM 1376 CB ALA B2061 0.348 25.139 20.411 1.00 19.50 C ATOM 1377 C ALAB2061 −0.655 23.464 22.015 1.00 20.28 C ATOM 1378 O ALA B2061 0.10322.952 22.841 1.00 20.05 O ATOM 1379 N PHE B2062 −1.896 23.832 22.3131.00 20.49 N ATOM 1380 CA PHE B2062 −2.419 23.620 23.659 1.00 21.41 CATOM 1381 CB PHE B2062 −3.738 24.382 23.880 1.00 21.26 C ATOM 1382 CGPHE B2062 −4.350 24.142 25.242 1.00 21.63 C ATOM 1383 CD1 PHE B2062−5.134 23.015 25.481 1.00 21.14 C ATOM 1384 CD2 PHE B2062 −4.092 25.00926.297 1.00 21.77 C ATOM 1385 CE1 PHE B2062 −5.646 22.756 26.745 1.0021.47 C ATOM 1386 CE2 PHE B2062 −4.603 24.757 27.576 1.00 22.09 C ATOM1387 CZ PHE B2062 −5.382 23.627 27.799 1.00 21.52 C ATOM 1388 C PHEB2062 −2.630 22.133 23.938 1.00 22.03 C ATOM 1389 O PHE B2062 −2.30321.655 25.022 1.00 22.28 O ATOM 1390 N SER B2063 −3.183 21.406 22.9701.00 22.94 N ATOM 1391 CA SER B2063 −3.403 19.972 23.135 1.00 24.34 CATOM 1392 CB SER B2063 −4.120 19.379 21.921 1.00 24.96 C ATOM 1393 OGSER B2063 −5.510 19.618 21.995 1.00 26.96 O ATOM 1394 C SER B2063 −2.08919.231 23.338 1.00 24.82 C ATOM 1395 O SER B2063 −2.053 18.192 23.9891.00 24.78 O ATOM 1396 N LYS B2064 −1.010 19.754 22.778 1.00 24.97 NATOM 1397 CA LYS B2064 0.266 19.091 22.952 1.00 26.19 C ATOM 1398 CB LYSB2064 1.201 19.454 21.802 1.00 25.92 C ATOM 1399 CG LYS B2064 0.72318.846 20.496 1.00 26.10 C ATOM 1400 CD LYS B2064 1.437 19.406 19.2931.00 26.40 C ATOM 1401 CE LYS B2064 2.890 19.016 19.272 1.00 25.79 CATOM 1402 NZ LYS B2064 3.444 19.339 17.935 1.00 26.57 N ATOM 1403 C LYSB2064 0.860 19.447 24.312 1.00 27.18 C ATOM 1404 O LYS B2064 1.44318.593 24.978 1.00 27.11 O ATOM 1405 N ALA B2065 0.680 20.696 24.7341.00 28.10 N ATOM 1406 CA ALA B2065 1.175 21.142 26.030 1.00 29.62 CATOM 1407 CB ALA B2065 0.851 22.617 26.241 1.00 29.09 C ATOM 1408 C ALAB2065 0.520 20.309 27.128 1.00 30.86 C ATOM 1409 O ALA B2065 1.12120.062 28.170 1.00 30.13 O ATOM 1410 N MET B2066 −0.721 19.890 26.8921.00 32.95 N ATOM 1411 CA MET B2066 −1.449 19.079 27.866 1.00 35.41 CATOM 1412 CB MET B2066 −2.957 19.167 27.626 1.00 35.78 C ATOM 1413 CGMET B2066 −3.588 20.479 28.047 1.00 36.88 C ATOM 1414 SD MET B2066−3.734 20.673 29.828 1.00 38.18 S ATOM 1415 CE MET B2066 −5.497 20.28830.048 1.00 38.92 C ATOM 1416 C MET B2066 −1.010 17.621 27.783 1.0036.81 C ATOM 1417 O MET B2066 −1.414 16.797 28.595 1.00 36.82 O ATOM1418 N GLY B2067 −0.178 17.311 26.798 1.00 38.52 N ATOM 1419 CA GLYB2067 −0.292 15.950 26.644 1.00 41.07 C ATOM 1420 C GLY B2067 −0.79414.998 26.187 1.00 42.84 C ATOM 1421 O GLY B2067 −1.321 14.214 26.9791.00 43.50 O ATOM 1422 N THR B2068 −1.140 15.077 24.908 1.00 44.30 NATOM 1423 CA THR B2068 −2.152 14.206 24.322 1.00 45.93 C ATOM 1424 CBTHP B2068 −3.410 14.994 23.903 1.00 45.92 C ATOM 1425 OG1 THR B2068−3.075 15.921 22.861 1.00 46.12 O ATOM 1426 CG2 THR B2068 −3.972 15.75825.093 1.00 46.09 C ATOM 1427 C THP B2068 −1.501 13.593 23.088 1.0047.07 C ATOM 1428 O THR B2068 −2.151 12.918 22.287 1.00 47.09 O ATOM1429 N GLY B2069 −0.202 13.862 22.957 1.00 48.53 N ATOM 1430 CA GLYB2069 0.599 13.356 21.853 1.00 49.83 C ATOM 1431 C GLY B2069 −0.08513.307 20.503 1.00 50.67 C ATOM 1432 O GLY B2069 −0.047 14.274 19.7411.00 51.10 O ATOM 1433 N ILE B2070 −0.699 12.166 20.208 1.00 51.17 NATOM 1434 CA ILE B2070 −1.405 11.948 18.952 1.00 51.53 C ATOM 1435 CBILE B2070 −1.574 10.427 18.668 1.00 51.94 C ATOM 1436 CG2 ILE B2070−0.221 9.804 18.341 1.00 51.87 C ATOM 1437 CG1 ILE B2070 −2.217 9.73719.882 1.00 52.15 C ATOM 1438 CD1 ILE B2070 −2.470 8.249 19.712 1.0052.43 C ATOM 1439 C ILE B2070 −2.792 12.590 18.979 1.00 51.42 C ATOM1440 O ILE B2070 −3.074 13.534 18.232 1.00 51.57 O ATOM 1441 N SER B2071−3.653 12.068 19.847 1.00 51.02 N ATOM 1442 CA SER B2071 −5.013 12.56619.967 1.00 50.61 C ATOM 1443 CB SER B2071 −5.803 11.680 20.938 1.0050.61 C ATOM 1444 OG SER B2071 −5.007 11.299 22.044 1.00 50.73 O ATOM1445 C SER B2071 −5.064 14.030 20.404 1.00 50.07 C ATOM 1446 O SER B2071−4.042 14.625 20.771 1.00 49.91 O ATOM 1447 N LYS B2072 −6.258 14.61220.340 1.00 49.03 N ATOM 1448 CA LYS B2072 −6.440 16.004 20.728 1.0047.71 C ATOM 1449 CB LYS B2072 −6.637 16.898 19.495 1.00 48.58 C ATOM1450 CG LYS B2072 −5.733 16.397 18.312 1.00 49.59 C ATOM 1451 CD LYSB2072 −6.215 17.358 17.087 1.00 50.30 C ATOM 1452 CE LYS B2072 −5.50016.909 15.820 1.00 50.97 C ATOM 1453 NZ LYS B2072 −6.051 17.588 14.6101.00 51.33 N ATOM 1454 C LYS B2072 −7.670 16.146 21.610 1.00 46.22 CATOM 1455 O LYS B2072 −8.484 15.229 21.742 1.00 46.03 O ATOM 1456 N LEUB2073 −7.787 17.322 22.208 1.00 44.70 N ATOM 1457 CA LEU B2073 −8.91517.658 23.048 1.00 42.68 C ATOM 1458 CB LEU B2073 −8.540 18.812 23.9751.00 42.47 C ATOM 1459 CG LEU B2073 −7.416 18.504 24.959 1.00 42.08 CATOM 1460 CD1 LEU B2073 −6.916 19.781 25.594 1.00 42.04 C ATOM 1461 CD2LEU B2073 −7.925 17.543 26.010 1.00 42.14 C ATOM 1462 C LEU B2073 −9.99918.116 22.083 1.00 41.35 C ATOM 1463 O LEU B2073 −9.750 18.273 20.8811.00 41.21 O ATOM 1464 N GLY B2074 −11.203 18.312 22.595 1.00 39.49 NATOM 1465 CA GLY B2074 −12.252 18.791 21.727 1.00 37.51 C ATOM 1466 CGLY B2074 −11.852 20.211 21.364 1.00 35.85 C ATOM 1467 O GLY B2074−11.493 20.998 22.240 1.00 35.43 O ATOM 1468 N PHE B2075 −11.878 20.54820.082 1.00 33.89 N ATOM 1469 CA PHE B2075 −11.524 21.900 19.704 1.0032.41 C ATOM 1470 CB PHE B2075 −11.287 21.990 18.194 1.00 32.43 C ATOM1471 CG PHE B2075 −9.846 21.778 17.802 1.00 32.87 C ATOM 1472 CD1 PHEB2075 −8.952 21.151 18.682 1.00 33.28 C ATOM 1473 CD2 PHE B2075 −9.37922.191 16.557 1.00 33.06 C ATOM 1474 CE1 PHE B2075 −7.616 20.941 18.3261.00 33.27 C ATOM 1475 CE2 PHE B2075 −8.047 21.987 16.187 1.00 33.20 CATOM 1476 CZ PHE B2075 −7.163 21.360 17.071 1.00 33.45 C ATOM 1477 C PHEB2075 −12.597 22.877 20.163 1.00 31.04 C ATOM 1478 O PHE B2075 −12.34024.072 20.277 1.00 30.78 O ATOM 1479 N GLN B2076 −13.787 22.357 20.4621.00 29.52 N ATOM 1480 CA GLN B2076 −14.897 23.185 20.929 1.00 28.06 CATOM 1481 CB GLN B2076 −16.226 22.493 20.630 1.00 27.83 C ATOM 1482 CGGLN B2076 −16.489 22.365 19.144 1.00 27.93 C ATOM 1483 CD GLN B2076−16.666 23.716 18.479 1.00 28.25 C ATOM 1484 OE1 GLN B2076 −16.17023.950 17.376 1.00 28.52 O ATOM 1485 NE2 GLN B2076 −17.387 24.613 19.1451.00 27.92 N ATOM 1486 C GLN B2076 −14.765 23.476 22.423 1.00 27.11 CATOM 1487 O GLN B2076 −15.536 24.241 23.000 1.00 26.54 O ATOM 1488 N ASPB2077 −13.768 22.860 23.037 1.00 26.23 N ATOM 1489 CA ASP B2077 −13.50523.059 24.447 1.00 26.09 C ATOM 1490 CB ASP B2077 −13.173 21.721 25.1081.00 27.19 C ATOM 1491 CG ASP B2077 −14.401 20.856 25.292 1.00 28.36 CATOM 1492 OD1 ASP B2077 −15.304 21.276 26.043 1.00 29.34 O ATOM 1493 OD2ASP B2077 −14.469 19.767 24.686 1.00 29.83 O ATOM 1494 C ASP B2077−12.354 24.041 24.614 1.00 24.96 C ATOM 1495 O ASP B2077 −11.917 24.32825.730 1.00 24.58 O ATOM 1496 N LEU B2078 −11.870 24.553 23.490 1.0023.44 N ATOM 1497 CA LEU B2078 −10.783 25.507 23.502 1.00 22.63 C ATOM1498 CB LEU B2078 −9.534 24.900 22.868 1.00 22.62 C ATOM 1499 CG LEUB2078 −8.989 23.599 23.468 1.00 22.75 C ATOM 1500 CD1 LEU B2078 −7.93323.010 22.543 1.00 22.77 C ATOM 1501 CD2 LEU B2078 −8.401 23.870 24.8411.00 22.96 C ATOM 1502 C LEU B2078 −11.200 26.741 22.726 1.00 22.37 CATOM 1503 O LEU B2078 −11.709 26.642 21.611 1.00 21.73 O ATOM 1504 N GLUB2079 −11.001 27.908 23.324 1.00 21.99 N ATOM 1505 CA GLU B2079 −11.34229.145 22.648 1.00 21.60 C ATOM 1506 CB GLU B2079 −12.624 29.740 23.2141.00 21.69 C ATOM 1507 CG GLU B2079 −13.132 30.922 22.421 1.00 22.30 CATOM 1508 CD GLU B2079 −14.459 31.412 22.937 1.00 23.08 C ATOM 1509 OE1GLU B2079 −14.499 31.893 24.089 1.00 24.19 O ATOM 1510 OE2 GLU B2079−15.462 31.311 22.201 1.00 22.86 O ATOM 1511 C GLU B2079 −10.216 30.14422.792 1.00 21.14 C ATOM 1512 O GLU B2079 −9.606 30.265 23.862 1.0021.43 O ATOM 1513 N VAL B2080 −9.940 30.852 21.705 1.00 20.42 N ATOM1514 CA VAL B2080 −8.892 31.850 21.691 1.00 20.15 C ATOM 1515 CB VALB2080 −7.728 31.418 20.780 1.00 19.96 C ATOM 1516 CG1 VAL B2080 −6.66232.517 20.735 1.00 19.66 C ATOM 1517 CG2 VAL B2080 −7.127 30.123 21.2971.00 19.86 C ATOM 1518 C VAL B2080 −9.436 33.187 21.211 1.00 20.63 CATOM 1519 O VAL B2080 −9.899 33.820 20.075 1.00 20.55 O ATOM 1520 N LEUB2081 −9.379 34.178 22.089 1.00 20.91 N ATOM 1521 CA LEU B2081 −9,85235.515 21.767 1.00 21.71 C ATOM 1522 CB LEU B2081 −10.913 35.953 22.7791.00 21.41 C ATOM 1523 CG LEU B2081 −12.150 35.049 22.846 1.00 21.70 CATOM 1524 COl LEU B2081 −13.145 35.618 23.864 1.00 20.86 C ATOM 1525 CG2LEU B2081 −12.788 34.947 21.451 1.00 20.91 C ATOM 1526 C LEU B2081−8.690 36.488 21.802 1.00 21.95 C ATOM 1527 O LEU B2081 −7.592 36.13522.255 1.00 22.11 O ATOM 1528 N ASN B2082 −8.927 37.700 21.302 1.0022.09 N ATOM 1529 CA ASN B2082 −7.912 38.754 21.334 1.00 22.53 C ATOM1530 CB ASN B2082 −7.809 39.483 19.992 1.00 23.53 C ATOM 1531 CG ASNB2082 −7.347 38.588 18.882 1.00 24.84 C ATOM 1532 001 ASN B2082 −6.35037.880 19.016 1.00 25.69 O ATOM 1533 ND2 ASN B2082 −8.066 38.613 17.7661.00 26.27 N ATOM 1534 C ASM B2082 −8.345 39.754 22.402 1.00 22.18 CATOM 1535 O ASN B2082 −9.528 40.069 22.514 1.00 21.35 O ATOM 1536 N ASNB2083 −7.391 40.244 23.186 1.00 22.35 N ATOM 1537 CA ASN B2083 −7.69941.215 24.227 1.00 22.53 C ATOM 1538 CB ASN B2083 −6.711 41.092 25.3911.00 21.65 C ATOM 1539 CG ASN B2083 −5.267 41.394 24.995 1.00 21.91 CATOM 1540 ODi ASN B2083 −4.338 41.115 25.762 1.00 22.04 O ATOM 1541 ND2ASN B2083 −5.068 41.963 23.808 1.00 20.96 N ATOM 1542 C ASN B2083 −7.67942.632 23.663 1.00 23.31 C ATOM 1543 O ASN B2083 −7.344 42.834 22.4931.00 23.42 O ATOM 1544 N GLU B2084 −8.037 43.605 24.498 1.00 23.94 NATOM 1545 CA GLU B2084 −8.062 45.012 24.098 1.00 24.84 C ATOM 1546 CBGLU B2084 −8.089 45.924 25.336 1.0026.09 C ATOM 1547 CG GLU B2084 −9.17145.622 26.355 1.00 28.21 C ATOM 1548 CD OLU B2084 −8.992 44.259 27.0141.00 30.57 C ATOM 1549 OE1 GLU B2084 −7.892 44.001 27.565 1.00 31.38 OATOM 1550 OE2 GLU B2084 −9.952 43.448 26.984 1.00 31.36 O ATOM 1551 CGLU B2084 −6.871 45.421 23.223 1.00 24.40 C ATOM 1552 O GLU B2084 −7.03346.197 22.292 1.00 24.89 O ATOM 1553 N ARG B2085 −5.683 44.905 23.5301.00 24.24 N ATOM 1554 CA ARG B2085 −4.464 45.245 22.782 1.00 24.07 CATOM 1555 CB ARG B2085 −3.237 45.139 23.688 1.00 24.81 C ATOM 1556 CGARG B2085 −3.375 45.824 25.022 1.00 26.63 C ATOM 1557 CD ARG B2085−2.090 45.727 25.844 1.00 27.63 C ATOM 1558 NE ARG B2085 −2.124 46.66826.962 1.00 28.81 N ATOM 1559 CZ ARG B2095 −2.915 46.532 28.016 1.0029.08 C ATOM 1560 NH1 ARG B2085 −3.725 45.489 28.090 1.00 30.38 N ATOM1561 NH2 ARG B2085 −2.915 47.441 28.984 1.00 29.49 N ATOM 1562 C ARGB2085 −4.201 44.386 21.548 1.00 23.45 C ATOM 1563 O ARG B2085 −3.23144.616 20.839 1.00 23.48 O ATOM 1564 N GLY B2086 −5.043 43.388 21.3041.00 22.86 N ATOM 1565 CA GLY B2086 −4.845 42.531 20.148 1.00 22.18 CATOM 1566 C GLY B2086 −4.106 41.231 20.442 1.00 22.02 C ATOM 1567 O GLYB2086 −3.935 40.391 19.557 1.00 22.97 O ATOM 1568 N ALA B2087 −3.65841.053 21.677 1.00 20.91 N ATOM 1569 CA ALA B2087 −2.948 39.836 22.0381.00 19.91 C ATOM 1570 CB ALA B2087 −2.196 40.028 23.362 1.00 19.31 CATOM 1571 C ALA B2087 −3.940 38.675 22.161 1.00 19.35 C ATOM 1572 O ALAB2087 −5.013 38.816 22.757 1.00 18.31 O ATOM 1573 N PRO B2088 −3.59837.520 21.566 1.00 19.16 N ATOM 1574 CB PRO B2088 −2.449 37.311 20.6561.00 19.16 C ATOM 1575 CA PRO B2088 −4.450 36.331 21.611 1.00 18.85 CATOM 1576 CB PRO B2088 −3.968 35.529 20.408 1.00 19.28 C ATOM 1577 CGPRO B2088 −2.478 35.817 20.403 1.00 18.72 C ATOM 1578 C PRO B2088 −4.22935.597 22.934 1.00 18.76 C ATOM 1579 O PRO B2088 −3.098 35.484 23.4041.00 18.99 O ATOM 1580 N TYR B2089 −5.310 35.108 23.533 1.00 18.27 NATOM 1581 CA TYR B2089 −5.230 34.394 24.804 1.00 17.56 C ATOM 1582 CBTYR B2089 −5.394 35.379 25.960 1.00 15.80 C ATOM 1583 CG TYR B2089−6.792 35.933 26.103 1.00 14.62 C ATOM 1584 CD1 TYR B2089 −7.684 35.40227.036 1.00 14.04 C ATOM 1585 CE1 TYR B2089 −8.983 35.916 27.160 1.0013.45 C ATOM 1586 CD2 TYR B2089 −7.231 36.991 25.294 1.00 13.76 C ATOM1587 CE2 TYR B2089 −8.507 37.499 25.405 1.00 12.48 C ATOM 1588 CZ TYRB2089 −9.381 36.964 26.336 1.00 13.07 C ATOM 1589 OH TYR B2089 −10.64937.475 26.433 1.00 12.87 O ATOM 1590 C TYR B2089 −6.333 33.349 24.8651.00 18.14 C ATOM 1591 O TYR B2089 −7.302 33.433 24.118 1.00 18.32 OATOM 1592 N PHE B2090 −6.196 32.360 25.741 1.00 18.75 N ATOM 1593 CA PHEB2090 −7.242 31.350 25.853 1.00 19.41 C ATOM 1594 CB PHE B2090 −6.68630.012 26.353 1.00 18.52 C ATOM 1595 CG PHE B2090 −6.044 29.187 25.2821.00 18.19 C ATOM 1596 CD1 PHE B2090 −4.716 29.402 24.912 1.00 17.08 CATOM 1597 CD2 PHE B2090 6.769 28.182 24.638 1.00 17.63 C ATOM 1598 CE1PHE B2090 −4.119 28.626 23.920 1.00 16.47 C ATOM 1599 CE2 PHE B2090−6.177 27.400 23.640 1.00 16.79 C ATOM 1600 CZ PHE B2090 −4.847 27.62523.284 1.00 16.73 C ATOM 1601 C PHE B2090 −8.334 31.806 26.802 1.0020.35 C ATOM 1602 O PHE B2090 −8.092 31.963 27.997 1.00 20.62 O ATOM1603 N SER B2091 −9.535 32.010 26.271 1.00 21.43 N ATOM 1604 CA SERB2091 −10.664 32.430 27.096 1.00 22.72 C ATOM 1605 CB SER B2091 −11.63533.293 26.278 1.00 22.59 C ATOM 1606 OG SER B2091 −12.173 32.566 25.1871.00 24.06 O ATOM 1607 C SER B2091 −11.385 31.194 27.651 1.00 23.50 CATOM 1608 O SER B2091 −12.133 31.289 28.623 1.00 23.39 O ATOM 1609 N GLNB2092 −11.154 30.041 27.024 1.00 24.05 N ATOM 1610 CA GLN B2092 −11.75728.784 27.458 1.00 25.18 C ATOM 1611 CB GLN B2092 −12.970 28.420 26.5911.00 26.15 C ATOM 1612 CG GLN B2092 −14.194 29.321 26.733 1.00 28.02 CATOM 1613 CD GLN B2092 −14.848 29.241 28.105 1.00 29.69 C ATOM 1614 OE1GLN B2092 −14.974 28.159 28.687 1.00 30.83 O ATOM 1615 NE2 GLN B2092−15.283 30.389 28.622 1.00 30.35 N ATOM 1616 C GLN 92092 −10.725 27.66127.354 1.00 25.31 C ATOM 1617 O GLN 92092 −10.029 27.541 26.343 1.0025.18 O ATOM 1618 N ALA B2093 −10.631 26.838 28.395 1.00 25.61 N ATOM1619 CA ALA B2093 −9.680 25.733 28.394 1.00 26.50 C ATOM 1620 CB ALA22093 −8.243 26.278 28.384 1.00 25.87 C ATOM 1621 C ALA 22093 −9.87624.805 29.587 1.00 27.03 C ATOM 1622 O ALA B2093 −10.200 25.252 30.6871.00 27.16 O ATOM 1623 N PRO B2094 −9.671 23.492 29.382 1.00 27.79 NATOM 1624 CD PRO B2094 −9.377 22.840 28.090 1.00 27.87 C ATOM 1625 CAPRO B2094 −9.824 22.497 30.452 1.00 28.17 C ATOM 1626 CB PRO B2094−9.970 21.191 29.681 1.00 27.97 C ATOM 1627 CG PRO B2094 −9.068 21.40828.501 1.00 27.75 C ATOM 1628 C PRO B2094 −8.611 22.489 31.384 1.0028.93 C ATOM 1629 O PRO B2094 −8.149 21.429 31.819 1.00 29.42 O ATOM1630 N PHE B2095 −8.099 23.676 31.690 1.00 29.04 N ATOM 1631 CA PHEB2095 −6.929 23.812 32.551 1.00 28.93 C ATOM 1632 CB PHE B2095 −5.70424.150 31.689 1.00 28.61 C ATOM 1633 CG PHE B2095 −4.416 24.266 32.4601.00 28.08 C ATOM 1634 CD1 PHE B2095 −3.697 25.457 32.454 1.00 27.74 CATOM 1635 CG2 PHE B2095 −3.918 23.185 33.187 1.00 27.48 C ATOM 1636 CBlPHE B2095 −2.503 25.574 33.158 1.00 27.44 C ATOM 1637 CB2 PHE B2095−2.730 23.292 33.893 1.00 27.21 C ATOM 1638 CZ PHE B2095 −2.018 24.49233.880 1.00 27.64 C ATOM 1639 C PHE B2095 −7.220 24.934 33.544 1.0029.17 C ATOM 1640 O PHE B2095 −7.922 25.893 33.211 1.00 29.61 O ATOM1641 N SER B2096 −6.690 24.821 34.758 1.00 28.80 N ATOM 1642 CA SERB2096 −6.931 25.837 35.771 1.00 28.67 C ATOM 1643 CB SER B2096 −7.37425.177 37.078 1.00 29.60 C ATOM 1644 OG SER B2096 −8.489 24.328 36.8591.00 31.74 O ATOM 1645 C SER B2096 −5.719 26.716 36.038 1.00 27.69 CATOM 1646 O SER B2096 −5.828 27.746 36.700 1.00 27.77 O ATOM 1647 N GLYB2097 −4.563 26.318 35.526 1.00 26.80 N ATOM 1648 CA GLY B2097 −3.37027.115 35.752 1.00 25.56 C ATOM 1649 C GLY B2097 −3.246 28.268 34.7711.00 24.43 C ATOM 1650 O GLY B2097 −4.224 28.686 34.155 1.00 23.36 OATOM 1651 N LYS B2098 −2.032 28.786 34.629 1.00 23.85 N ATOM 1652 CA LYSB2098 −1.786 29.886 33.707 1.00 23.16 C ATOM 1653 CB LYS B2098 −0.65630.789 34.212 1.00 24.15 C ATOM 1654 CG LYS B2098 −1.025 31.639 35.4081.00 25.14 C ATOM 1655 CD LYS B2098 0.036 32.693 35.659 1.00 26.88 CATOM 1656 CE LYS B2098 −0.288 33.524 36.895 1.00 27.83 C ATOM 1657 NZLYS B2098 −0.224 32.680 38.126 1.00 28.96 N ATOM 1658 C LYS B2098 −1.40629.332 32.353 1.00 21.88 C ATOM 1659 O LYS B2098 −0.604 28.402 32.2611.00 21.71 O ATOM 1660 N ILE B2099 −1.997 29.905 31.310 1.00 20.39 NATOM 1661 CA ILE B2099 −1.723 29.494 29.941 1.00 19.37 C ATOM 1662 CBILE B2099 −3.027 29.186 29.165 1.00 19.23 C ATOM 1663 CG2 ILE B2099−2.695 28.629 27.779 1.00 18.49 C ATOM 1664 CG1 ILE B2099 −3.878 28.18229.950 1.00 18.74 C ATOM 1665 CD1 ILE B2099 −5.199 27.892 29.299 1.0018.23 C ATOM 1666 C ILE B2099 −0.997 30.621 29.221 1.00 18.65 C ATOM1667 O ILE B2099 −1.570 31.683 28.973 1.00 18.86 O ATOM 1668 N TRP B21000.273 30.401 28.907 1.00 17.78 N ATOM 1669 CA TRP B2100 1.043 31.40728.195 1.00 17.08 C ATOM 1670 CB TRP B2100 2.477 31.487 28.735 1.0015.80 C ATOM 1671 CG TRP B2100 2.533 31.922 30.180 1.00 15.68 C ATOM1672 CD2 TRP B2100 2.423 33.264 30.679 1.00 15.05 C ATOM 1673 CE2 TRPB2100 2.466 33.189 32.093 1.00 15.31 C ATOM 1674 CE3 TRP B2100 2.28934.522 30.070 1.00 15.15 C ATOM 1675 CD1 TRP B2100 2.636 31.111 31.2841.00 15.45 C ATOM 1676 NE1 TRP B2100 2.595 31.868 32.432 1.00 15.26 NATOM 1677 CZ2 TRP B2100 2.384 34.328 32.912 1.00 15.02 C ATOM 1678 CZ3TRP B2100 2.204 35.658 30.883 1.00 15.47 C ATOM 1679 CH2 TRP B2100 2.25335.548 32.291 1.00 15.54 C ATOM 1680 C TRP B2100 1.027 31.028 26.7231.00 17.16 C ATOM 1681 O TRP B2100 1.627 30.041 26.311 1.00 17.52 O ATOM1682 N LEU B2101 0.314 31.821 25.937 1.00 17.56 N ATOM 1683 CA LEU B21010.180 31.575 24.508 1.00 17.56 C ATOM 1684 CB LEU B2101 −1.304 31.45424.137 1.00 17.63 C ATOM 1685 CG LEU B2101 −1.641 31.497 22.635 1.0018.34 C ATOM 1686 CD1 LEU B2101 −1.241 30.157 21.964 1.00 17.98 C ATOM1687 CD2 LEU B2101 −3.132 31.768 22.444 1.00 17.63 C ATOM 1688 C LEUB2101 0.789 32.685 23.681 1.00 17.40 C ATOM 1689 O LEU B2101 0.77033.849 24.075 1.00 17.23 O ATOM 1690 N SER B2102 1.332 32.312 22.5291.00 17.67 N ATOM 1691 CA SER B2102 1.892 33.274 21.602 1.00 17.46 CATOM 1692 CB SER B2102 3.366 33.551 21.892 1.00 17.36 C ATOM 1693 OG SERB2102 3.797 34.687 21.150 1.00 17.27 O ATOM 1694 C SER B2102 1.73132.739 20.185 1.00 17.83 C ATOM 1695 O SER B2102 1.984 31.563 19.9191.00 17.13 O ATOM 1696 N ILE B2103 1.286 33.616 19.288 1.00 18.64 N ATOM1697 CA ILE B2103 1.084 33.270 17.888 1.00 19.37 C ATOM 1698 CB ILEB2103 −0.429 33.275 17.515 1.00 19.72 C ATOM 1699 CG2 ILE B2103 −0.62532.778 16.079 1.00 19.83 C ATOM 1700 CG1 ILE B2103 −1.213 32.382 18.4801.00 20.18 C ATOM 1701 CD1 ILE B2103 −2.722 32.470 18.314 1.00 20.28 CATOM 1702 C ILE B2103 1.813 34.299 17.014 1.00 19.77 C ATOM 1703 O ILEB2103 1.857 35.489 17.330 1.00 18.81 O ATOM 1704 N SER B2104 2.39633.818 15.925 1.00 20.35 N ATOM 1705 CA SER B2104 3.096 34.673 14.9741.00 21.48 C ATOM 1706 CB SER B2104 4.603 34.675 15.268 1.00 21.45 CATOM 1707 OG SER B2104 5.328 35.484 14.351 1.00 21.11 O ATOM 1708 C SERB2104 2.826 34.069 13.598 1.00 22.45 C ATOM 1709 O SER B2104 2.49232.884 13.488 1.00 22.26 O ATOM 1710 N HIS B2105 2.949 34.872 12.5491.00 23.91 N ATOM 1711 CA HIS B2105 2.725 34.348 11.207 1.00 25.44 CATOM 1712 CB HIS B2105 1.235 34.372 10.867 1.00 26.52 C ATOM 1713 CG HISB2105 0.682 35.754 10.693 1.00 27.10 C ATOM 1714 CD2 HIS B2105 0.35336.451 9.577 1.00 27.93 C ATOM 1715 ND1 HIS B2105 0.427 36.594 11.7551.00 27.73 N ATOM 1716 CE1 HIS B2105 −0.036 37.747 11.302 1.00 27.61 CATOM 1717 NE2 HIS B2105 −0.091 37.686 9.984 1.00 27.60 N ATOM 1718 C HISB2105 3.467 35.117 10.123 1.00 25.84 C ATOM 1719 O HIS B2105 3.83636.274 10.303 1.00 25.76 O ATOM 1720 N THR B2106 3.688 34.444 9.001 1.0026.43 N ATOM 1721 CA THR B2106 4.314 35.051 7.834 1.00 27.12 C ATOM 1722CB THR B2106 5.546 34.261 7.341 1.00 27.09 C ATOM 1723 OG1 THR B21065.137 32.968 6.888 1.00 26.88 O ATOM 1724 CG2 THR B2106 6.576 34.1208.452 1.00 27.18 C ATOM 1725 C THR B2106 3.213 34.953 6.777 1.00 27.59 CATOM 1726 O THR B2106 2.059 34.688 7.116 1.00 28.11 O ATOM 1727 N ASPB2107 3.553 35.148 5.508 1.00 27.85 N ATOM 1728 CA ASP B2107 2.55435.068 4.449 1.00 28.22 C ATOM 1729 CB ASP B2107 3.085 35.722 3.170 0.0528.14 C ATOM 1730 CG ASP B2107 3.275 37.220 3.316 0.05 28.09 C ATOM 1731OD1 ASP B2107 2.276 37.926 3.569 0.05 28.04 O ATOM 1732 OD2 ASP B21074.422 37.693 3.177 0.05 28.08 O ATOM 1733 C ASP B2107 2.116 33.632 4.1381.00 28.63 C ATOM 1734 O ASP B2107 0.995 33.408 3.684 1.00 28.77 O ATOM1735 N GLN B2108 2.988 32.662 4.392 1.00 28.69 N ATOM 1736 CA GLN B21082.663 31.272 4.093 1.00 29.21 C ATOM 1737 CB GLN B2108 3.753 30.6663.201 1.00 30.96 C ATOM 1738 CG GLN B2108 4.217 31.565 2.059 1.00 32.72C ATOM 1739 CD GLN B2108 5.386 30.967 1.282 1.00 34.31 C ATOM 1740 OE1GLN B2108 5.195 30.201 0.328 1.00 34.84 O ATOM 1741 NE2 GLN B2108 6.60531.306 1.699 1.00 34.53 N ATOM 1742 C GLN B2108 2.482 30.366 5.308 1.0028.68 C ATOM 1743 O GLN B2108 1.819 29.337 5.215 1.00 28.89 O ATOM 1744N PHE B2109 3.068 30.741 6.441 1.00 27.66 N ATOM 1745 CA PHE B2109 2.98529.916 7.641 1.00 26.50 C ATOM 1746 CB PHE B2109 4.347 29.287 7.953 1.0026.61 C ATOM 1747 CG PHE B2109 4.860 28.387 6.875 1.00 27.11 C ATOM 1748CD1 PHE B2109 5.577 28.907 5.799 1.00 27.30 C ATOM 1749 CD2 PHE B21094.599 27.020 6.913 1.00 26.71 C ATOM 1750 CE1 PHE B2109 6.026 28.0734.773 1.00 27.50 C ATOM 1751 CE2 PHE B2109 5.045 26.180 5.893 1.00 27.16C ATOM 1752 CZ PHE B2109 5.757 26.706 4.823 1.00 27.50 C ATOM 1753 C PHEB2109 2.524 30.648 8.883 1.00 25.59 C ATOM 1754 O PHE B2109 2.625 31.8728.967 1.00 25.67 O ATOM 1755 N VAL B2110 2.016 29.881 9.843 1.00 24.04 NATOM 1756 CA VAL B2110 1.580 30.435 11.114 1.00 23.42 C ATOM 1757 CB VALB2110 0.045 30.435 11.267 1.00 23.14 C ATOM 1758 CG1 VAL B2110 −0.49829.016 11.276 1.00 23.49 C ATOM 1759 CG2 VAL B2110 −0.327 31.151 12.5351.00 23.40 C ATOM 1760 C VAL B2110 2.201 29.562 12.188 1.00 22.98 C ATOM1761 O VAL B2110 2.371 28.364 11.996 1.00 23.38 O ATOM 1762 N THR B21112.555 30.161 13.314 1.00 22.66 N ATOM 1763 CA THR B2111 3.175 29.40214.390 1.00 22.51 C ATOM 1764 CB THR B2111 4.674 29.721 14.459 1.0023.02 C ATOM 1765 OG1 THR B2111 5.310 28.830 15.373 1.00 25.57 O ATOM1766 CG2 THR B2111 4.891 31.148 14.928 1.00 23.27 C ATOM 1767 C THRB2111 2.531 29.714 15.735 1.00 21.17 C ATOM 1768 O THR B2111 2.01330.807 15.939 1.00 21.65 O ATOM 1769 N ALA B2112 2.565 28.748 16.6491.00 19.97 N ATOM 1770 CA ALA B2112 1.986 28.928 17.985 1.00 18.49 CATOM 1771 CB ALA B2112 0.549 28.422 18.009 1.00 16.81 C ATOM 1772 C ALAB2112 2.805 28.227 19.073 1.00 17.74 C ATOM 1773 O ALA B2112 3.37527.168 18.857 1.00 16.72 O ATOM 1774 N SER B2113 2.860 28.834 20.2511.00 17.84 N ATOM 1775 CA SER B2213 3.597 28.250 21.365 1.00 17.93 CATOM 1776 CB SER B2113 4.985 28.893 21.495 1.00 17.90 C ATOM 1777 OG SERB2113 5.742 28.263 22.512 1.00 17.60 O ATOM 1778 C SER B2113 2.80528.439 22.653 1.00 17.35 C ATOM 1779 O SER B2113 2.262 29.510 22.9051.00 17.22 O ATOM 1780 N VAL B2114 2.749 27.382 23.452 1.00 16.89 N ATOM1781 CA VAL B2114 2.020 27.383 24.708 1.00 16.75 C ATOM 1782 CB VALB2114 0.718 26.533 24.612 1.00 16.63 C ATOM 1783 CG1 VAL B2114 0.11226.347 25.999 1.00 16.16 C ATOM 1784 CG2 VAL B2114 −0.298 27.205 23.6751.00 16.25 C ATOM 1785 C VAL B2114 2.862 26.799 25.835 1.00 17.45 C ATOM1786 O VAL B2114 3.503 25.750 25.680 1.00 16.99 O ATOM 1787 N ILE B21152.863 27.497 26.966 1.00 17.80 N ATOM 1788 CA ILE B2115 3.566 27.03728.156 1.00 18.72 C ATOM 1789 CB ILE B2115 4.689 28.008 28.602 1.0018.37 C ATOM 1790 CG2 ILE B2115 5.385 27.452 29.846 1.00 18.27 C ATOM1791 CG1 ILE B2115 5.708 28.205 27.480 1.00 18.40 C ATOM 1792 CD1 ILEB2115 6.745 29.289 27.786 1.00 17.55 C ATOM 1793 C ILE B2115 2.51527.000 29.260 1.00 19.25 C ATOM 1794 O ILE B2115 1.858 28.004 29.5241.00 19.38 O ATOM 1795 N LEU B2116 2.336 25.846 29.884 1.00 20.55 N ATOM1796 CA LEU B2116 1.374 25.735 30.968 1.00 22.30 C ATOM 1797 CB LEUB2116 0.628 24.404 30.902 1.00 21.86 C ATOM 1798 CG LEU B2116 −0.14724.159 29.603 1.00 22.00 C ATOM 1799 CD1 LEU B2116 −0.976 22.893 29.7321.00 21.49 C ATOM 1800 CD2 LEU B2116 −1.050 25.359 29.303 1.00 21.93 CATOM 1801 C LEU B2116 2.123 25.864 32.290 1.00 24.11 C ATOM 1802 O LEUB2116 3.209 25.299 32.472 1.00 23.89 O ATOM 1803 N GLU B2117 1.54426.621 33.210 1.00 26.00 N ATOM 1804 CA GLU B2117 2.177 26.840 34.4931.00 28.60 C ATOM 1805 CB GLU B2117 2.746 28.258 34.531 1.00 28.59 CATOM 1806 CG GLU B2117 3.418 28.627 35.829 1.00 30.48 C ATOM 1807 CD GLUB2117 4.079 29.997 35.771 1.00 31.11 C ATOM 1808 OE1 GLU B2117 3.39530.972 35.385 1.00 31.07 O ATOM 1809 OE2 GLU B2117 5.281 30.092 36.1151.00 31.14 O ATOM 1810 C GLU B2117 1.217 26.601 35.659 1.00 30.07 C ATOM1811 O GLU B2117 0.029 26.938 35.595 1.00 29.34 O ATOM 1812 N GLU B21181.742 26.006 36.726 1.00 32.11 N ATOM 1813 CA GLU B2118 0.926 25.71237.889 1.00 34.40 C ATOM 1814 CB GLU B2118 0.997 24.223 38.212 1.0035.62 C ATOM 1815 CG GLU B2118 −0.294 23.679 38.772 1.00 37.98 C ATOM1816 CD GLU B2118 −1.458 23.905 37.825 1.00 39.13 C ATOM 1817 OE1 GLUB2118 −1.403 23.398 36.682 1.00 39.94 O ATOM 1818 OE2 GLU B2118 −2.42224.596 38.222 1.00 40.32 O ATOM 1819 C GLU B2118 1.387 26.515 39.0901.00 35.21 C ATOM 1820 O GLU B2118 2.611 26.552 39.343 1.00 35.67 O ATOM1821 OXT GLU B2118 0.507 27.088 39.767 1.00 36.45 O TER 1822 GLU B2118ATOM 1823 CB MET C3003 14.254 28.191 38.580 1.00 31.28 C ATOM 1824 CGMET C3003 15.448 27.262 38.618 1.00 32.93 C ATOM 1825 SD MET C300316.870 27.987 39.434 1.00 35.68 S ATOM 1826 CE MET C3003 16.438 27.67241.140 1.00 34.95 C ATOM 1827 C MET C3003 13.519 27.087 36.482 1.0029.25 C ATOM 1828 O MET C3003 13.901 25.920 36.332 1.00 28.76 O ATOM1829 N MET C3003 12.435 26.519 38.666 1.00 30.53 N ATOM 1830 CA METC3003 13.052 27.596 37.845 1.00 30.20 C ATOM 1831 N ILE C3004 13.49127.976 35.493 1.00 28.16 N ATOM 1832 CA ILE C3004 13.945 27.636 34.1491.00 27.31 C ATOM 1833 CB ILE C3004 13.377 28.604 33.084 1.00 27.05 CATOM 1834 CG2 ILE C3004 14.103 28.413 31.761 1.00 26.26 C ATOM 1835 CG1ILE C3004 11.876 28.372 32.919 1.00 26.90 C ATOM 1836 CD1 ILE C300411.203 29.374 31.996 1.00 27.09 C ATOM 1837 C ILE C3004 15.452 27.77534.170 1.00 26.61 C ATOM 1838 O ILE C3004 15.970 28.755 34.685 1.0026.80 O ATOM 1839 N VAL C3005 16.153 26.794 33.617 1.00 26.02 N ATOM1840 CA VAL C3005 17.611 26.822 33.581 1.00 25.10 C ATOM 1841 CB VALC3005 18.221 25.644 34.396 1.00 25.36 C ATOM 1842 CG1 VAL C3005 17.82025.766 35.869 1.00 25.11 C ATOM 1843 CG2 VAL C3005 17.755 24.306 33.8331.00 24.57 C ATOM 1844 C VAL C3005 18.124 26.747 32.152 1.00 24.50 CATOM 1845 O VAL C3005 19.327 26.640 31.928 1.00 25.44 O ATOM 1846 N GLYC3006 17.212 26.805 31.186 1.00 23.63 N ATOM 1847 CA GLY C3006 17.61226.736 29.791 1.00 22.31 C ATOM 1848 C GLY C3006 16.446 26.762 28.8201.00 21.49 C ATOM 1849 O GLY C3006 15.332 26.348 29.156 1.00 21.47 OATOM 1850 N HIS C3007 16.700 27.254 27.609 1.00 20.33 N ATOM 1851 CA HISC3007 15.664 27.336 26.582 1.00 19.44 C ATOM 1852 GB HIS C3007 14.80628.591 26.785 1.00 18.31 C ATOM 1853 CG HIS C3007 13.749 28.777 25.7411.00 18.22 C ATOM 1854 CD2 HIS C3007 13.411 29.857 24.997 1.00 18.17 CATOM 1855 ND1 HIS C3007 12.871 27.778 25.384 1.00 18.32 N ATOM 1856 CE1HIS C3007 12.036 28.233 24.467 1.00 18.15 C ATOM 1857 NE2 HIS C300712.342 29.492 24.215 1.00 18.03 N ATOM 1858 C HIS C3007 16.288 27.35725.196 1.00 18.96 C ATOM 1859 O HIS C3007 17.200 28.125 24.940 1.0019.65 O ATOM 1860 N GLY C3008 15.795 26.504 24.307 1.00 18.27 N ATOM1861 CA GLY C3008 16.340 26.468 22.965 1.00 17.73 C ATOM 1862 C GLYC3008 15.307 26.061 21.932 1.00 17.73 C ATOM 1863 O GLY C3008 14.39825.274 22.215 1.00 16.98 O ATOM 1864 N ILE C3009 15.426 26.620 20.7351.00 17.47 N ATOM 1865 CA ILE C3009 14.512 26.281 19.658 1.00 18.23 CATOM 1866 CB ILE C3009 13.483 27.414 19.340 1.00 17.95 C ATOM 1867 CG2ILE C3009 12.743 27.836 20.604 1.00 17.06 C ATOM 1868 CG1 ILE C300914.192 28.608 18.683 1.00 17.87 C ATOM 1869 CD1 ILE C3009 13.233 29.65318.104 1.00 18.30 C ATOM 1870 C ILE C3009 15.327 26.029 18.406 1.0019.18 C ATOM 1871 O ILE C3009 16.516 26.345 18.345 1.00 18.80 O ATOM1872 N ASP C3010 14.682 25.439 17.413 1.00 20.69 N ATOM 1873 CA ASPC3010 15.330 25.188 16.144 1.00 22.71 C ATOM 1874 CB ASP C3010 16.25123.974 16.216 1.00 23.72 C ATOM 1875 CG ASP C3010 16.949 23.710 14.8991.00 24.96 C ATOM 1876 OD1 ASP C3010 17.840 24.501 14.528 1.00 26.04 OATOM 1877 OD2 ASP C3010 16.598 22.724 14.219 1.00 26.67 O ATOM 1878 CASP C3010 14.307 24.963 15.045 1.00 23.50 C ATOM 1879 O ASP C3010 13.23924.407 15.278 1.00 23.37 O ATOM 1880 N ILE C3011 14.645 25.428 13.8511.00 24.39 N ATOM 1881 CA ILE C3011 13.796 25.259 12.695 1.00 25.77 CATOM 1882 CB ILE C3011 13.178 26.600 12.239 1.00 25.68 C ATOM 1883 CG2ILE C3011 14.270 27.609 11.941 1.00 24.95 C ATOM 1884 CG1 ILE C301112.274 26.364 11.022 1.00 25.90 O ATOM 1885 CD1 ILE C3011 11.308 27.50110.737 1.00 25.60 O ATOM 1886 C ILE C3011 14.701 24.681 11.616 1.0027.06 O ATOM 1887 O ILE C3011 15.856 25.091 11.476 1.00 27.35 O ATOM1888 N GLU C3012 14.182 23.700 10.885 1.00 28.16 N ATOM 1889 CA GLUC3012 14.937 23.048 9.829 1.00 29.36 C ATOM 1890 CB GLU C3012 15.41021.664 10.278 1.00 30.33 C ATOM 1891 CG GLU C3012 16.347 21.633 11.4671.00 31.58 C ATOM 1892 CD GLU C3012 17.722 22.207 11.164 1.00 32.87 CATOM 1893 OE1 GLU C3012 18.082 22.322 9.965 1.00 32.65 O ATOM 1894 OE2GLU C3012 18.447 22.529 12.138 1.00 32.87 O ATOM 1895 C GLU C3012 14.09722.872 8.580 1.00 29.90 O ATOM 1896 O GLU C3012 12.906 22.548 8.647 1.0029.35 O ATOM 1897 N GLU C3013 14.729 23.095 7.435 1.00 31.00 N ATOM 1898CA GLU C3013 14.067 22.913 6.153 1.00 32.07 C ATOM 1899 CB GLU C301314.782 23.722 5.075 1.00 33.32 C ATOM 1900 CG GLU C3013 14.202 23.5643.684 1.00 35.05 C ATOM 1901 CD GLU C3013 15.142 24.089 2.614 1.00 36.48C ATOM 1902 OE1 GLU C3013 15.645 25.228 2.761 1.00 36.82 O ATOM 1903 OE2GLU C3013 15.376 23.365 1.622 1.00 37.39 O ATOM 1904 C GLU C3013 14.20621.418 5.873 1.00 31.77 C ATOM 1905 O GLU C3013 15.306 20.877 5.914 1.0031.08 O ATOM 1906 N LEU C3014 13.098 20.750 5.614 1.00 32.39 N ATOM 1907CA LEU C3014 13.130 19.318 5.360 1.00 33.65 C ATOM 1908 CB LEU C301411.718 18.794 5.080 1.00 33.57 C ATOM 1909 CG LEU C3014 10.813 18.6856.313 1.00 34.16 C ATOM 1910 CD1 LEU C3014 9.416 18.252 5.906 1.00 34.65C ATOM 1911 CD2 LEU C3014 11.404 17.680 7.280 1.00 34.38 C ATOM 1912 CLEU C3014 14.069 18.946 4.220 1.00 34.37 C ATOM 1913 O LEU C3014 14.73617.913 4.271 1.00 34.47 O ATOM 1914 N ALA C3015 14.128 19.801 3.204 1.0035.44 N ATOM 1915 CA ALA C3015 14.982 19.572 2.047 1.00 36.79 C ATOM1916 CB ALA C3015 14.749 20.655 1.011 1.00 36.53 C ATOM 1917 C ALA C301516.457 19.511 2.418 1.00 37.84 C ATOM 1918 O ALA C3015 17.215 18.7371.831 1.00 38.53 O ATOM 1919 N SER C3016 16.868 20.322 3.391 1.00 39.07N ATOM 1920 CA SER C3016 18.258 20.349 3.838 1.00 40.09 C ATOM 1921 CBSER C3016 18.473 21.478 4.847 1.00 40.11 C ATOM 1922 OG SER C3016 18.17222.734 4.271 1.00 41.50 O ATOM 1923 C SER C3016 18.628 19.026 4.481 1.0040.95 C ATOM 1924 O SER C3016 19.757 18.552 4.340 1.00 41.12 O ATOM 1925N ILE C3017 17.683 18.428 5.197 1.00 41.82 N ATOM 1926 CA ILE C301717.951 17.158 5.849 1.00 43.16 C ATOM 1927 CB ILE C3017 16.799 16.7686.795 1.00 42.90 C ATOM 1928 CG2 ILE C3017 17.170 15.527 7.598 1.0042.32 C ATOM 1929 CG1 ILE C3017 16.518 17.924 7.759 1.00 43.05 C ATOM1930 CD1 ILE C3017 17.709 18.332 8.597 1.00 42.53 C ATOM 1931 C ILEC3017 18.165 16.076 4.789 1.00 44.24 C ATOM 1932 O ILE C3017 19.03315.215 4.941 1.00 44.09 O ATOM 1933 N GLU C3018 17.383 16.128 3.713 1.0045.44 N ATOM 1934 CA GLU C3018 17.530 15.158 2.637 1.00 47.05 C ATOM1935 CB GLU C3018 16.516 15.411 1.524 1.00 47.54 C ATOM 1936 CG GLUC3018 15.158 14.805 1.755 1.00 48.25 C ATOM 1937 CD GLU C3018 14.38314.664 0.463 1.00 48.87 C ATOM 1938 QEl GLU C3018 14.159 15.686 −0.2201.00 49.40 O ATOM 1939 022 GLU C3018 14.005 13.525 0.126 1.00 49.49 OATOM 1940 C GLU C3018 18.929 15.261 2.048 1.00 47.90 C ATOM 1941 O GLUC3018 19.696 14.299 2.083 1.00 47.96 O ATOM 1942 N SER C3019 19.24816.429 1.495 1.00 48.89 N ATOM 1943 CA SER C3019 20.560 16.658 0.9051.00 49.72 C ATOM 1944 CB SER C3019 20.815 18.152 0.713 1.00 49.87 CATOM 1945 OG SER C3019 19.977 18.685 −0.295 1.00 50.04 O ATOM 1946 C SERC3019 21.614 16.078 1.825 1.00 50.34 C ATOM 1947 O SER C3019 22.50615.362 1.380 1.00 50.79 O ATOM 1948 N ALA C3020 21.504 16.380 3.114 1.0050.84 N ATOM 1949 CA ALA C3020 22.461 15.860 4.083 1.00 51.57 C ATOM1950 CB ALA C3020 22.054 16.266 5.491 1.00 51.45 C ATOM 1951 C ALA C302022.511 14.338 3.960 1.00 52.20 C ATOM 1952 O ALA C3020 23.585 13.7523.811 1.00 52.03 O ATOM 1953 N VAL C3021 21.337 13.711 4.013 1.00 53.10N ATOM 1954 CA VAL C3021 21.212 12.259 3.897 1.00 53.96 C ATOM 1955 CBVAL C3021 19.730 11.818 3.969 1.00 53.97 C ATOM 1956 CG1 VAL C302119.609 10.329 3.671 1.00 54.14 C ATOM 1957 CG2 VAL C3021 19.165 12.1245.340 1.00 53.98 C ATOM 1958 C VAL C3021 21.788 11.793 2.566 1.00 54.57C ATOM 1959 O VAL C3021 22.424 10.740 2.481 1.00 54.43 O ATOM 1960 N THRC3022 21.553 12.591 1.530 1.00 55.21 N ATOM 1961 CA THR C3022 22.04112.293 0.194 1.00 55.84 C ATOM 1962 CB THR C3022 21.456 13.283 −0.8311.00 55.80 C ATOM 1963 OG1 THR C3022 20.034 13.124 −0.878 1.00 55.98 OATOM 1964 CG2 THR C3022 22.036 13.036 −2.214 1.00 55.79 C ATOM 1965 CTHR C3022 23.566 12.355 0.155 1.00 56.35 C ATOM 1966 O THR C3022 24.21311.386 −0.230 1.00 56.58 O ATOM 1967 N ARG C3023 24.135 13.489 0.5571.00 56.81 N ATOM 1968 CA ARG C3023 25.586 13.650 0.567 1.00 57.20 CATOM 1969 CB ARG C3023 25.966 15.015 1.151 1.00 57.25 C ATOM 1970 CG ARGC3023 27.463 15.289 1.151 1.00 57.60 C ATOM 1971 CD ARG C3023 27.78216.762 1.388 1.00 57.64 C ATOM 1972 NE ARG C3023 27.410 17.222 2.7220.05 57.76 N ATOM 1973 CZ ARG C3023 27.609 18.460 3.163 0.05 57.81 CATOM 1974 NH1 ARG C3023 28.176 19.364 2.374 0.05 57.84 N ATOM 1975 NH2ARG C3023 27.245 18.796 4.393 0.05 57−.82 N ATOM 1976 C ARG C3023 26.20312.522 1.390 1.00 57.47 C ATOM 1977 O ARG C3023 26.328 11.402 0.903 1.0057.73 O ATOM 1978 N HIS C3024 26.592 12.806 2.630 1.00 57.66 N ATOM 1979CA HIS C3024 27.168 11.773 3.486 1.00 57.79 C ATOM 1980 CB HIS C302427.968 12.404 4.627 0.05 57.91 C ATOM 1981 CG HIS C3024 29.442 12.4494.375 0.05 58.00 C ATOM 1982 CG2 HIS C3024 30.301 13.491 4.278 0.0558.04 C ATOM 1983 ND1 HIS C3024 30.198 11.312 4.187 0.05 58.04 N ATOM1984 CBl HIS C3024 31.459 11.651 3.986 0.05 58.06 C ATOM 1985 NE2 HISC3024 31.549 12.968 4.036 0.05 58.07 N ATOM 1986 C HIS C3024 26.06910.873 4.054 1.00 57.96 C ATOM 1987 O HIS C3024 25.413 11.223 5.038 1.0058.10 O ATOM 1988 N GLU C3025 25.874 9.710 3.435 1.00 57.92 N ATOM 1989CA GLTJ C3025 24.846 8.773 3.879 1.00 57.71 C ATOM 1990 CB GLU C302524.824 7.535 2.976 1.00 58.27 C ATOM 1991 CG GLU C3025 25.979 6.5713.189 1.00 59.11 C ATOM 1992 CD GLU C3025 25.784 5.259 2.446 1.00 59.59C ATOM 1993 OE1 GLU C3025 24.749 4.592 2.673 1.00 59.65 O ATOM 1994 OE2GLU C3025 26.665 4.893 1.637 1.00 59.98 O ATOM 1995 C GLU C3025 25.0298.341 5.336 1.00 57.11 C ATOM 1996 O GLU C3025 24.089 7.857 5.974 1.0057.33 O ATOM 1997 N GLY C3026 26.238 8.508 5.861 1.00 56.15 N ATOM 1998CA GLY C3026 26.486 8.136 7.242 1.00 55.03 C ATOM 1999 C GLY C302625.890 9.170 8.177 1.00 54.19 C ATOM 2000 O GLY C3026 26.023 9.081 9.3981.00 54.12 O ATOM 2001 N PHF C3027 25.227 10.160 7.589 1.00 53.18 N ATOM2002 CA PHE C3027 24.601 11.238 8.343 1.00 52.05 C ATOM 2003 CB PHEC3027 23.817 12.142 7.386 1.00 52.10 C ATOM 2004 CG PHE C3027 23.12913.289 8.059 1.00 52.03 C ATOM 2005 CD1 PHE C3027 23.859 14.233 8.7681.00 51.96 C ATOM 2006 CG2 PHE C3027 21.743 13.427 7.984 1.00 52.34 CATOM 2007 CBl PHE C3027 23.221 15.304 9.398 1.00 52.41 C ATOM 2008 CB2PHE C3027 21.092 14.492 8.609 1.00 52.33 C ATOM 2009 CZ PHE C3027 21.83315.434 9.319 1.00 52.40 C ATOM 2010 C PHE C3027 23.676 10.720 9.443 1.0051.01 C ATOM 2011 O PHE C3027 23.914 10.957 10.628 1.00 51.01 O ATOM2012 N ALA C3028 22.631 10.002 9.042 1.00 49.81 N ATOM 2013 CA ALA C302821.648 9.463 9.979 1.00 48.74 C ATOM 2014 CB ALA C3028 20.608 8.6459.231 1.00 48.50 C ATOM 2015 C ALA C3028 22.240 8.630 11.104 1.00 48.04C ATOM 2016 O ALA C3028 21.865 8.802 12.266 1.00 47.95 O ATOM 2017 N LYSC3029 23.156 7.726 10.767 1.00 47.14 N ATOM 2018 CA LYS C3029 23.7656.874 11.779 1.00 46.13 C ATOM 2019 CB LYS C3029 24.681 5.833 11.1261.00 46.10 C ATOM 2020 CG LYS C3029 25.918 6.410 10.460 0.05 46.12 CATOM 2021 CD LYS C3029 26.810 5.310 9.907 0.05 46.11 C ATOM 2022 CB LYSC3029 28.065 5.884 9.269 0.05 46.11 C ATOM 2023 NZ LYS C3029 28.8736.675 10.238 0.05 46.11 N ATOM 2024 G LYS C3029 24.548 7.709 12.789 1.0045.54 C ATOM 2025 O LYS C3029 24.739 7.299 13.936 1.00 45.54 O ATOM 2026N ARG C3030 24.997 8.883 12.361 1.00 44.50 N ATOM 2027 CA ARG C303025.747 9.770 13.243 1.00 43.62 C ATOM 2028 CB ARG C3030 26.703 10.65012.425 1.00 43.71 C ATOM 2029 CG ARG C3030 28.071 10.019 12.194 0.0543.64 C ATOM 2030 CD ARG C3030 28.410 9.914 10.717 0.05 43.63 C ATOM2031 NE ARG C3030 28.407 11.214 10.051 0.05 43.58 N ATOM 2032 CZ ARGC3030 28.653 11.389 8.756 0.05 43.55 C ATOM 2033 NH1 ARG C3030 28.92310.347 7.983 0.05 43.53 N ATOM 2034 NH2 ARG C3030 28.626 12.608 8.2340.05 43.55 N ATOM 2035 C ARG C3030 24.819 10.651 14.071 1.00 42.89 CATOM 2036 O ARG C3030 25.183 11.099 15.158 1.00 42.93 O ATOM 2037 N VALC3031 23.616 10.885 13.556 1.00 41.77 N ATOM 2038 CA VAL C3031 22.63711.724 14.237 1.00 40.54 C ATOM 2039 CB VAL C3031 21.761 12.464 13.2131.00 40.55 C ATOM 2040 CG1 VAL C3031 20.717 13.298 13.926 1.00 40.68 CATOM 2041 CG2 VAL C3031 22.631 13.339 12.328 1.00 40.57 C ATOM 2042 CVAL C3031 21.727 10.941 15.180 1.00 39.76 C ATOM 2043 O VAL C3031 21.37311.418 16.256 1.00 39.22 O ATOM 2044 N LEU C3032 21.353 9.736 14.7711.00 39.10 N ATOM 2045 CA LEU C3032 20.470 8.905 15.572 1.00 38.53 CATOM 2046 CB LEU C3032 19.453 8.223 14.656 1.00 38.36 C ATOM 2047 CG LEUC3032 18.612 9.150 13.767 1.00 38.42 C ATOM 2048 CD1 LEU C3032 17.6718.308 12.912 1.00 38.50 C ATOM 2049 CG2 LEU C3032 17.819 10.131 14.6221.00 37.90 C ATOM 2050 C LEU C3032 21.217 7.848 16.378 1.00 38.18 C ATOM2051 O LEU C3032 22.395 7.585 16.134 1.00 38.41 O ATOM 2052 N THR C303320.530 7.263 17.356 1.00 37.76 N ATOM 2053 CA THR C3033 21.105 6.19318.166 1.00 37.32 C ATOM 2054 CB THR C3033 20.636 6.248 19.638 1.0037.17 C ATOM 2055 OCi THR C3033 19.233 5.967 19.704 1.00 37.15 O ATOM2056 CG2 THR C3033 20.900 7.612 20.236 1.00 37.54 C ATOM 2057 C THRC3033 20.546 4.918 17.537 1.00 37.05 C ATOM 2058 O THR C3033 19.7254.992 16.623 1.00 36.86 O ATOM 2059 N ALA C3034 20.976 3.759 18.026 1.0037.00 N ATOM 2060 CA ALA C3034 20.502 2.481 17.495 1.00 36.98 C ATOM2061 CB ALA C3034 21.121 1.324 18.279 1.00 36.85 C ATOM 2062 C ALA C303418.978 2.384 17.538 1.00 36.93 C ATOM 2063 O ALA C3034 18.331 2.15416.516 1.00 36.95 O ATOM 2064 N LEU C3035 18.401 2.553 18.721 1.00 37.04N ATOM 2065 CA LEU C3035 16.951 2.480 18.844 1.00 37.28 C ATOM 2066 CBLEU C3035 16.522 2.844 20.271 1.00 37.10 C ATOM 2067 CG LEU C3035 15.1832.291 20.770 0.05 37.08 C ATOM 2068 CD1 LEU C3035 14.994 2.675 22.2290.05 37.00 C ATOM 2069 CG2 LEU C3035 14.040 2.822 19.922 0.05 37.02 CATOM 2070 C LEU C3035 16.322 3.442 17.828 1.00 37.52 C ATOM 2071 O LEUC3035 15.418 3.065 17.084 1.00 37.65 O ATOM 2072 N GLU C3036 16.8144.678 17.790 1.00 37.89 N ATOM 2073 CA GLU C3036 16.299 5.679 16.8541.00 38.14 C ATOM 2074 CB GLU C3036 17.007 7.031 17.063 1.00 37.82 CATOM 2075 CG GLU C3036 16.486 7.857 18.244 1.00 37.71 C ATOM 2076 CD GLUC3036 17.305 9.128 18.490 1.00 37.80 C ATOM 2077 OEl GLU C3036 16.8659.989 19.283 1.00 37.10 O ATOM 2078 OE2 GLU C3036 18.397 9.265 17.8961.00 37.62 O ATOM 2079 C GLU C3036 16.462 5.232 15.398 1.00 38.18 C ATOM2080 O GLU C3036 15.629 5.551 14.553 1.00 38.25 O ATOM 2081 N MET C303717.533 4.499 15.104 1.00 38.56 N ATOM 2082 CA MET C3037 17.769 4.02213.743 1.00 39.53 C ATOM 2083 CB MET C3037 19.196 3.495 13.591 1.0040.21 C ATOM 2084 CG MET C3037 20.230 4.576 13.312 1.00 41.61 C ATOM2085 SD MET C3037 19.932 5.428 11.726 1.00 43.58 S ATOM 2086 CB METC3037 20.794 4.327 10.578 1.00 42.57 C ATOM 2087 C MET C3037 16.7822.935 13.337 1.00 39.68 C ATOM 2088 O MET C3037 16.356 2.881 12.186 1.0039.73 O ATOM 2089 N GLU C3038 16.421 2.072 14.284 1.00 39.82 N ATOM 2090CA GLU C3038 15.473 0.995 14.012 1.00 39.88 C ATOM 2091 CB GLU C303815.205 0.190 15.289 1.00 39.75 C ATOM 2092 CG GLU C3038 16.451 −0.42815.905 0.05 39.71 C ATOM 2093 CD GLU C3038 16.163 −1.139 17.213 0.0539.67 C ATOM 2094 OE1 GLU C3038 15.344 −2.083 17.210 0.05 39.64 O ATOM2095 OE2 GLU C3038 16.755 −0.755 18.243 0.05 39.61 O ATOM 2096 C GLUC3038 14.175 1.609 13.500 1.00 40.09 C ATOM 2097 O GLU C3038 13.5561.105 12.559 1.00 40.19 O ATOM 2098 N ARG C3039 13.774 2.709 14.126 1.0040.05 N ATOM 2099 CA ARG C3039 12.560 3.418 13.744 1.00 40.26 C ATOM2100 CB ARG C3039 12.230 4.466 14.811 1.00 40.88 C ATOM 2101 CG ARGC3039 11.106 5.425 14.468 1.00 41.43 C ATOM 2102 CD ARG C3039 9.7564.739 14.377 1.00 42.67 C ATOM 2103 NE ARG C3039 8.673 5.723 14.425 1.0043.58 N ATOM 2104 CZ ARG C3039 7.394 5.459 14.169 1.00 43.85 C ATOM 2105NH1 ARG C3039 7.007 4.231 13.838 1.00 43.59 N ATOM 2106 NH2 ARG C30396.498 6.435 14.234 1.00 44.15 N ATOM 2107 C ARG C3039 12.755 4.09012.384 1.00 39.98 C ATOM 2108 O ARG C3039 11.891 4.009 11.506 1.00 39.45O ATOM 2109 N PHE C3040 13.901 4.745 12.216 1.00 40.04 N ATOM 2110 CAPHE C3040 14.218 5.440 10.968 1.00 40.26 C ATOM 2111 CB PHE C3040 15.6036.074 11.061 1.00 40.27 C ATOM 2112 CG PHE C3040 16.022 6.804 9.814 1.0040.95 C ATOM 2113 CD1 PHE C3040 15.431 8.015 9.466 1.00 41.11 C ATOM2114 CG2 PHE C3040 17.013 6.282 8.989 1.00 41.10 C ATOM 2115 CBl PHEC3040 15.822 8.699 8.315 1.00 41.43 C ATOM 2116 CB2 PHE C3040 17.4126.956 7.835 1.00 41.44 C ATOM 2117 CZ PHE C3040 16.815 8.169 7.497 1.0041.61 C ATOM 2118 C PHE C3040 14.181 4.507 9.756 1.00 40.43 C ATOM 2119O PHE C3040 13.467 4.757 8.784 1.00 39.60 O ATOM 2120 N THR C3041 14.9563.429 9.833 1.00 40.82 N ATOM 2121 CA THR C3041 15.043 2.459 8.749 1.0041.42 C ATOM 2122 CB THR C3041 16.154 1.435 9.018 1.00 41.55 C ATOM 2123OG1 THR C3041 15.782 0.597 10.121 1.00 42.56 O ATOM 2124 CG2 THR C304117.450 2.149 9.351 1.00 41.22 C SLAYER ATOM 2125 C THR C3041 13.7491.702 8.463 1.00 41.42 C ATOM 2126 O THR C3041 13.630 1.072 7.415 1.0041.80 O ATOM 2127 N SER C3042 12.783 1.757 9.377 1.00 41.30 N ATOM 2128CA SER C3042 11.521 1.059 9.152 1.00 41.35 C ATOM 2129 CB SER C304210.998 0.445 10.454 1.00 41.25 C ATOM 2130 OG SER C3042 10.501 1.44211.324 1.00 42.03 O ATOM 2131 C SER C3042 10.469 1.996 6.569 1.00 41.30C ATOM 2132 0 SER C3042 9.334 1.589 8.311 1.00 41.45 O ATOM 2133 N LEUC3043 10.850 3.255 8.373 1.00 41.13 N ATOM 2134 CA LEU C3043 9.956 4.2627.808 1.00 40.94 C ATOM 2135 CB LEU C3043 10.026 5.566 8.618 1.00 40.70C ATOM 2136 CG LEU C3043 9.382 5.618 10.012 1.00 40.56 C ATOM 2137 COlLEU C3043 9.835 6.871 10.735 1.00 40.07 C ATOM 2138 CG2 LEU C3043 7.8595.586 9.891 1.00 40.06 . C ATOM 2139 C LEU C3043 10.398 4.528 6.375 1.0041.07 C ATOM 2140 0 LEU C3043 11.494 4.128 5.978 1.00 40.93 O ATOM 2141N LYS C3044 9.550 5.203 5.604 1.00 41.26 N ATOM 2142 CA LYS C3044 9.8715.513 4.214 1.00 41.42 C ATOM 2143 CB LYS C3044 9.481 4.346 3.307 1.0042.49 C ATOM 2144 CG LYS C3044 1.982 4.199 3.107 1.00 43.64 C ATOM 2145CD LYS C3044 7.678 3.191 2.012 1.00 45.17 C ATOM 2146 CB LYS C3044 6.2063.228 1.616 1.00 45.99 C ATOM 2147 NZ LYS C3044 5.900 2.249 0.535 1.0047.05 N ATOM 2148 G LYS C3044 9.147 6.768 3.739 1.00 40.92 C ATOM 2149 0LYS C3044 8.191 7.219 4.365 1.00 40.90 O ATOM 2150 N GLY C3045 9.6057.820 2.621 1.00 40.22 N ATOM 2151 CA GLY C3045 8.986 8.510 2.072 1.0039.26 C ATOM 2152 C GLY C3045 9.182 9.736 2.937 1.00 38.68 C ATOM 2153 0GLY C3045 10.142 9.829 3.694 1.00 38.24 0 ATOM 2154 N ARG C3046 8.26010.683 2.818 1.00 38.56 N ATOM 2155 CA ARG C3046 8.318 11.921 3.589 1.0038.49 C ATOM 2156 CB ARG C3046 7.107 12.793 3.251 1.00 38.44 C ATOM 2157CG ARG C3046 7.104 14.158 3.912 0.05 38.46 C ATOM 2158 CD ARG C30465.887 14.963 3.483 0.05 38.40 C ATOM 2159 NE ARG C3046 5.874 15.2002.042 0.05 38.36 N ATOM 2160 CZ ARG C3046 4.887 15.809 1.393 0.05 38.32C ATOM 2161 NH1 ARG C3046 4.963 15.982 0.081 0.05 38.29 N ATOM 2162 NH2ARG C3046 3.822 16.241 2.055 0.05 38.31 N ATOM 2163 C ARG C3046 8.37211.647 5.093 1.00 38.25 C ATOM 2164 0 ARG C3046 9.027 12.365 5.830 1.0038.13 O ATOM 2165 N ARG C3047 7.696 10.595 5.538 1.00 38.32 N ATOM 2166CA ARG C3047 7.673 10.234 6.953 1.00 38.52 C ATOM 2167 CB ARG C30476.727 9.051 7.169 1.00 39.67 C ATOM 2168 CG ARG C3047 5.251 9.432 7.2251.00 41.67 C ATOM 2169 CD ARG C3047 4.369 8.277 6.767 1.00 43.70 C ATOM2170 NE ARG C3047 3.141 8.152 7.550 1.00 45.24 N ATOM 2171 CZ ARG C30473.112 7.824 8.840 1.00 46.12 C ATOM 2172 NH1 ARG C3047 4.248 7.589 9.4951.00 46.08 N ATOM 2173 NH2 ARG C3047 1.947 7.722 9.474 1.00 45.94 N ATOM2174 C ARG C3047 9.042 9.906 7.554 1.00 38.04 C ATOM 2175 0 ARG C30479.287 −10.174 8.731 1.00 37.75 O ATOM 2176 N GLN C3048 9.931 9.820 6.7571.00 37.49 N ATOM 2177 CA GLN C3048 11.258 8.966 7.251 1.00 36.91 C ATOM2178 CB GLN C3048 11.912 7.919 6.349 1.00 36.94 C ATOM 2179 CG GLN C304813.283 7.496 6.849 1.00 37.10 C ATOM 2180 CD GLN C3048 14.092 6.7445.813 1.00 37.40 C ATOM 2181 OE1 GLN C3048 14.233 7.196 4.680 1.00 37.42O ATOM 2182 NE2 GLN C3048 14.643 5.600 6.202 1.00 37.18 N ATOM 2183 CGLN C3048 12.186 10.176 7.367 1.00 36.61 C ATOM 2184 0 GLN C3048 12.97110.284 8.315 1.00 36.44 O ATOM 2185 N ILE C3049 12.101 11.082 6.403 1.0035.91 N ATOM 2186 CA ILE U3049 12.932 12.271 6.429 1.00 35.80 C ATOM2187 CB ILE U3049 12.906 12.991 5.054 1.00 36.41 C ATOM 2188 CG2 ILEU3049 11.482 13.209 4.607 1.00 37.11 C ATOM 2189 001 ILE U3049 13.67814.307 5.136 1.00 36.64 C ATOM 2190 CD1 ILE U3049 15.150 14.108 5.4331.00 37.22 C ATOM 2191 C ILE U3049 12.436 13.201 7.542 1.00 35.41 C ATOM2192 0 ILE U3049 13.231 13.824 8.254 1.00 35.47 O ATOM 2193 N GLU C305011.119 13.280 7.707 1.00 34.48 N ATOM 2194 CA GLU C3050 10.546 14.1188.756 1.00 33.55 C ATOM 2195 CB GLU C3050 9.023 14.074 8.699 1.00 34.18C ATOM 2196 CO GLU C3050 8.471 14.609 7.410 1.00 36.22 C ATOM 2197 CDGLU C3050 7.005 14.309 7.242 1.00 37.41 C ATOM 2198 OE1 GLU C3050 6.54313.291 7.807 1.00 38.55 O ATOM 2199 OE2 GLU C3050 6.318 15.078 6.5311.00 37.87 O ATOM 2200 C GLU C3050 11.018 13.620 10.116 1.00 32.30 CATOM 2201 0 GLU C3050 11.275 14.412 11.023 1.00 31.96 O ATOM 2202 N TYRC3051 11.130 12.303 10.251 1.00 30.44 N ATOM 2203 CA TYR C3051 11.57411.715 11.501 1.00 29.38 C ATOM 2204 CB TYR C3051 11.438 10.191 11.4331.00 28.33 C ATOM 2205 CG TYR C3051 11.936 9.478 12.675 1.00 27.96 CATOM 2206 CD1 TYR C3051 13.234 8.964 12.741 1.00 27.15 C ATOM 2207 CE1TYR C3051 13.712 8.371 13.904 1.00 26.96 C ATOM 2208 CG2 TYR C305111.127 9.373 13.809 1.00 27.47 C ATOM 2209 CB2 TYR C3051 11.593 8.78814.967 1.00 27.13 C ATOM 2210 CZ TYR 03051 12.885 8.290 15.014 1.0027.21 C ATOM 2211 OH TYR C3051 13.344 7.735 16.187 1.00 27.00 O ATOM2212 C TYR 03051 13.019 12.117 11.818 1.00 29.01 C ATOM 2213 0 TYR C305113.342 12.486 12.946 1.00 28.83 0 ATOM 2214 N LEU C3052 13.886 12.06310.812 1.00 28.73 N ATOM 2215 CA LEU C3052 15.287 12.417 11.009 1.0028.07 C ATOM 2216 CB LEU C3052 16.105 12.059 9.761 1.00 27.77 C ATOM2217 CO LEU C3052 17.603 12.372 9.816 1.00 28.06 C ATOM 2218 CD1 LEUC3052 18.267 11.639 10.972 1.00 28.26 C ATOM 2219 CG2 LEU C3052 18.24111.957 8.516 1.00 28.46 C ATOM 2220 C LEU C3052 15.419 13.909 11.3111.00 27.59 C ATOM 2221 O LEU C3052 16.156 14.309 12.217 1.00 26.99 OATOM 2222 N ALA C3053 14.704 14.727 10.544 1.00 27.06 N ATOM 2223 CA ALAC3053 14.743 16.168 10.738 1.00 26.76 C ATOM 2224 GB ALA 03053 13.89816.852 9.691 1.00 26.56 C ATOM 2225 C ALA 03053 14.223 16.489 12.1341.00 26.71 C ATOM 2226 O ALA C3053 14.802 17.298 12.854 1.00 26.43 OATOM 2227 N GLY C3054 13.130 15.831 12.510 1.00 26.77 N ATOM 2228 CA GLYC3054 12.541 16.043 13.815 1.00 26.67 C ATOM 2229 C GLY C3054 13.51215.753 14.934 1.00 26.53 C ATOM 2230 0 GLY C3054 13.611 16.521 15.8821.00 26.44 O ATOM 2231 N ARG C3055 14.231 14.643 14.836 1.00 26.68 NATOM 2232 CA ARG C3055 15.198 −14.290 15.870 1.00 26.82 C ATOM 2233 GBARG C3055 15.705 12.868 15.666 1.00 26.65 C ATOM 2234 GO ARG C305514.968 11.843 16.498 1.00 26.91 C ATOM 2235 CD ARG C3055 13.458 11.92216.298 1.00 27.49 C ATOM 2236 NE ARG C3055 12.759 11.110 17.292 1.0027.69 N ATOM 2237 CZ ARG 03055 11.442 11.086 17.454 1.00 27.76 C ATOM2238 NH1 ARG C3055 10.662 11.831 16.685 1.00 27.51 N ATOM 2239 NH2 ARG03055 10.906 10.324 18.398 1.00 28.13 N ATOM 2240 C ARG C3055 16.36015.260 15.869 1.00 26.96 C ATOM 2241 0 ARG C3055 16.834 15.667 16.9281.00 26.54 O ATOM 2242 N TRP C3056 16.816 15.631 14.676 1.00 27.71 NATOM 2243 CA TRP C3056 17.917 16.575 14.556 1.00 28.70 C ATOM 2244 CBTRP C3056 18.247 16.837 13.082 1.00 30.14 C ATOM 2245 CG TRP C305619.074 18.069 12.881 1.00 32.25 C ATOM 2246 CG2 TRP C3056 20.495 18.12912.703 1.00 33.03 C ATOM 2247 CB2 TRP C3056 20.854 19.497 12.662 1.0033.33 C ATOM 2248 CB3 TRP C3056 21.500 17.163 12.579 1.00 33.56 C ATOM2249 COl TRP C3056 18.639 19.370 12.930 1.00 32.92 C ATOM 2250 NEl TRPC3056 19.704 20.230 12.803 1.00 33.50 N ATOM 2251 CZ2 TRP C3056 22.17519.920 12.505 1.00 33.41 C ATOM 2252 CZ3 TRP C3056 22.818 17.587 12.4221.00 33.92 C ATOM 2253 CH2 TRP C3056 23.141 18.954 12.367 1.00 33.82 CATOM 2254 C TRFKC3OS6 17.498 17.875 15.230 1.00 28.10 C ATOM 2255 0 TRPC3056 18.144 18.357 16.163 1.00 27.48 O ATOM 2256 N SER C3057 16.39718.429 14.749 1.00 27.65 N ATOM 2257 CA SER C3057 15.868 19.667 15.2881.00 27.54 C ATOM 2258 CB SER C3057 14.513 19.959 14.654 1.00 27.86 CATOM 2259 OG SER C3057 14.233 21.344 14.718 1.00 29.93 O ATOM 2260 C SERC3057 15.731 19.622 16.812 1.00 26.85 C ATOM 2261 0 SER C3057 16.05920.588 17.503 1.00 27.24 O ATOM 2262 N ALA C3058 15.257 18.501 17.3401.00 25.77 N ATOM 2263 CA ALA C3058 15.080 18.369 18.780 1.00 25.50 CATOM 2264 CB ALA C3058 14.334 17.077 19.094 1.00 25.02 C ATOM 2265 C ALAC3058 16.411 18.409 19.546 1.00 25.26 C ATOM 2266 0 ALA C3058 16.51319.024 20.607 1.00 24.25 O ATOM 2267 N LYS C3059 17.430 17.752 19.0001.00 25.32 N ATOM 2268 CA LYS C3059 18.736 17.704 19.646 1.00 25.14 CATOM 2269 CB LYS C3059 19.568 16.577 19.035 1.00 24.87 C ATOM 2270 CGLYS C3059 18.928 15.218 19.254 1.00 24.63 C ATOM 2271 CD LYS C305919.667 14.091 18.570 1.00 24.80 C ATOM 2272 CB LYS C3059 18.998 12.74618.869 1.00 24.92 C ATOM 2273 NZ LYS C3059 19.674 11.614 18.185 1.0024.83 N ATOM 2274 G LYS C3059 19.466 19.033 19.547 1.00 25.56 C ATOM2275 0 LYS C3059 20.262 19.388 20.415 1.00 25.33 O ATOM 2276 N GLU C306019.183 19.784 18.493 1.00 26.00 N ATOM 2277 CA GLU C3060 19.818 21.07618.326 1.00 26.76 C ATOM 2278 CB GLU C3060 19.568 21.618 16.919 1.0028.10 C ATOM 2279 CG GLU C3060 20.545 22.717 16.530 1.00 31.38 C ATOM2280 CD GLU C3060 22.005 22.278 16.691 1.00 33.19 C ATOM 2281 OEI GLUC3060 22.444 21.369 15.947 1.00 33.60 O ATOM 2282 OE2 GLU C3060 22.70922.839 17.569 1.00 34.17 O ATOM 2283 C GLU C3060 19.243 22.023 19.3771.00 26.31 C ATOM 2284 0 GLU C3060 19.985 22.698 20.089 1.00 25.94 OATOM 2285 N ALA C3061 17.914 22.048 19.477 1.00 25.95 N ATOM 2286 CA ALAC3061 17.221 22.899 20.442 1.00 25.01 C ATOM 2287 CB ALA C3061 15.71222.700 20.342 1.00 24.05 C ATOM 2288 C ALA C3061 17.696 22.562 21.8461.00 24.62 C ATOM 2289 0 ALA C3061 17.925 23.457 22.663 1.00 24.28 OATOM 2290 N PE−LE C3062 17.837 21.271 22.129 1.00 24.17 N ATOM 2291 CAPHE C3062 18.301 20.850 23.440 1.00 24.63 C ATOM 2292 CB PHE C306218.224 19.321 23.605 1.00 24.68 C ATOM 2293 CG PHE C3062 18.875 18.82824.871 1.00 24.04 C ATOM 2294 CD1 PHE C3062 20.238 18.538 24.900 1.0024.34 C ATOM 2295 CG2 PHE C3062 18.152 18.756 26.053 1.00 23.91 C ATOM2296 CBl PHE C3062 20.872 18.189 26.093 1.00 24.30 C ATOM 2297 CB2 PHEC3062 18.774 18.411 27.255 1.00 24.14 C ATOM 2298 CZ PHE C3062 20.13918.128 27.274 1.00 24.07 C ATOM 2299 C PHE C3062 19.732 21.316 23.7011.00 24.85 C ATOM 2300 0 PHE C3062 20.054 21.744 24.804 .1.00 24.51 OATOM 2301 N SER C3063 20.589 21.219 22.689 1.00 25.44 N ATOM 2302 CA SERC3063 21.976 21.650 22.933 1.00 26.48 C ATOM 2303 CB SER C3063 22.77721.312 21.576 1.00 26.81 C ATOM 2304 OG SER C3063 22.872 19.910 21.4031.00 28.20 O ATOM 2305 C SER C3063 22.059 23.149 23.082 1.00 26.77 CATOM 2306 0 SER C3063 22.891 23.614 23.859 1.00 26.78 O ATOM 2307 N LYSC3064 21.194 23.902 22.416 1.00 26.78 N ATOM 2308 CA LYS C3064 21.18825.342 22.565 1.00 27.25 C ATOM 2309 CB LYS C3064 20.379 25.973 21.4311.00 26.90 C ATOM 2310 CG LYS C3064 20.971 25.696 20.059 1.00 26.47 CATOM 2311 CD LYS C3064 20.066 26.159 18.938 1.00 26.20 C ATOM 2312 CBLYS C3064 19.799 27.664 18.988 1.00 26.50 C ATOM 2313 NZ LYS C306418.996 28.088 17.806 1.00 26.49 N ATOM 2314 G LYS C3064 20.616 25.71823.923 1.00 28.08 C ATOM 2315 0 LYS C3064 20.987 26.738 24.500 1.0027.79 O ATOM 2316 N ALA C3065 19.717 24.882 24.433 1.00 29.11 N ATOM2317 CA ALA C3065 19.111 25.124 25.735 1.00 30.40 C ATOM 2318 CB ALAC3065 17.957 24.163 25.968 1.00 29.37 C ATOM 2319 C ALA C3065 20.17924.932 26.804 1.00 31.79 C ATOM 2320 O ALA C3065 20.228 25.668 27.7861.00 31.85 O ATOM 2321 N MET C3066 21.035 23.939 26.595 1.00 33.85 NATOM 2322 CA MET C3066 22.114 23.628 27.524 1.00 36.16 C ATOM 2323 CBMET C3066 22.666 22.232 27.242 1.00 36.40 C ATOM 2324 CG MET C306621.804 21.097 27.752 1.00 37.31 C ATOM 2325 SD MET C3066 21.824 20.99329.551 1.00 38.61 S ATOM 2326 CB MET C3066 23.502 20.468 29.811 1.0038.12 C ATOM 2327 C MET C3066 23.247 24.638 27.413 1.00 37.57 C ATOM2328 0 MET C3066 23.958 24.893 28.379 1.00 37.83 O ATOM 2329 N GLY C306723.411 25.209 26.226 1.00 39.17 N ATOM 2330 CA GLY C3067 24.470 26.17726.024 1.00 41.14 C ATOM 2331 C GLY C3067 25.772 25.475 25.697 1.0042.59 C ATOM 2332 0 GLY C3067 26.831 25.822 26.226 1.00 42.74 O ATOM2333 N THR C3068 25.687 24.476 24.825 1.00 43.64 N ATOM 2334 CA THRC3068 26.853 23.710 24.418 1.00 44.94 C ATOM 2335 CB THR C3068 26.72322.243 24.877 1.00 45.62 C ATOM 2336 OGi THR C3068 27.927 21.529 24.5591.00 46.68 O ATOM 2337 CG2 THR C3068 25.539 21.572 24.188 1.00 45.83 CATOM 2338 C THR C3068 26.994 23.755 22.898 1.00 45.32 C ATOM 2339 0 THRC3068 26.027 24.200 22.242 1.00 45.93 O ATOM 2340 OXT THR C3068 28.05723.348 22.377 1.00 45.68 O TER 2341 THR C3068 ATOM 2342 C GLY C307425.582 13.730 21.033 1.00 50.05 C ATOM 2343 0 GLY C3074 24.831 13.33321.925 1.00 50.04 O ATOM 2344 N GLY C3074 27.008 15.502 22.091 1.0050.49 N ATOM 2345 CA GLY C3074 26.990 14.201 21.354 1.00 50.33 C ATOM2346 N PHE C3075 25.218 13.780 19.755 1.00 49.73 N ATOM 2347 CA PHEC3075 23.894 13.345 19.328 1.00 49.39 C ATOM 2348 CB PHE C3075 23.74013.548 17.818 1.00 49.61 C ATOM 2349 CG PHE C3075 23.196 14.902 17.4471.00 50.02 C ATOM 2350 COl PHE C3075 23.555 16.036 18.178 1.00 50.35 CATOM 2351 CG2 PHE C3075 22.316 15.045 16.382 1.00 50.13 C ATOM 2352 CBlPHE C3075 23.040 17.294 17.854 1.00 50.43 C ATOM 2353 CB2 PHE C307521.794 16.297 16.047 1.00 50.56 C ATOM 2354 CZ PHE C3075 22.156 17.42416.784 1.00 50.60 C ATOM 2355 C PHE C3075 23.644 11.894 19.710 1.0048.79 C ATOM 2356 O PHE C3075 22.530 11.528 20.073 1.00 48.53 O ATOM2357 N GLN C3076 24.694 11.082 19.642 1.00 48.39 N ATOM 2358 CA GLNC3076 24.602 9.671 19.998 1.00 47.89 C ATOM 2359 CB GLN C3076 25.9058.944 19.643 1.00 48.47 C ATOM 2360 CG GLN C3076 26.287 9.049 18.1751.00 49.29 C ATOM 2361 CD GLN C3076 25.242 8.441 17.260 1.00 49.81 CATOM 2362 OE1 GLN C3076 25.206 8.731 16.065 1.00 50.75 O ATOM 2363 NE2GLN C3076 24.391 7.584 17.815 1.00 49.76 N ATOM 2364 C GLN C3076 24.3519.560 21.492 1.00 47.10 C ATOM 2365 0 GLN C3076 24.003 8.493 22.000 1.0047.45 O ATOM 2366 N ASP C3077 24.533 10.676 22.190 1.00 45.97 N ATOM2367 CA ASP C3077 24.331 10.727 23.631 1.00 44.90 C ATOM 2368 CB ASPC3077 25.397 11.612 24.271 1.00 46.44 C ATOM 2369 CG ASP C3077 26.80011.083 24.036 1.00 47.82 C ATOM 2370 001 ASP C3077 27.081 9.951 24.4991.00 48.20 O ATOM 2371 002 ASP C3077 27.610 11.794 23.388 1.00 48.48 OATOM 2372 C ASP C3077 22.950 11.252 23.975 1.00 43.23 C ATOM 2373 0 ASPC3077 22.557 11.280 25.140 1.00 43.47 O ATOM 2374 N LEU C3078 22.21911.675 22.950 1.00 41.15 N ATOM 2375 CA LEU C3078 20.869 12.193 23.1291.00 38.63 C ATOM 2376 CB LELJ C3078 20.754 13.610 22.558 1.00 38.12 CATOM 2377 CG LEU C3078 21.787 14.645 23.005 1.00 37.91 C ATOM 2378 COlLEU C3078 21.511 15.974 22.313 1.00 37.65 C ATOM 2379 CG2 LEU C307821.735 14.801 24.508 1.00 37.75 C ATOM 2380 C LEU C3078 19.921 11.27222.376 1.00 36.97 C ATOM 2381 0 LEU C3078 20.225 10.833 21.269 1.0036.76 O ATOM 2382 N GLU C3079 18.778 10.974 22.979 1.00 34.99 N ATOM2383 CA GLU C3079 17.793 10.112 22.338 1.00 33.02 C ATOM 2384 CB GLUC3079 17.937 8.676 22.842 1.00 33.31 C ATOM 2385 CO GLU C3079 16.8187.753 22.412 1.00 34.12 C ATOM 2386 CD GLU C3079 17.129 6.298 22.6911.00 34.85 C ATOM 2387 OE1 GLU C3079 17.897 5.701 21.908 1.00 34.18 OATOM 2388 OE2 GLU C3079 16.616 5.754 23.699 1.00 35.70 O ATOM 2389 C GLUC3079 16.365 10.598 22.566 1.00 31.51 C ATOM 2390 0 GLU C3079 15.95510.880 23.695 1.00 31.00 O ATOM 2391 N VAL C3080 15.618 10.707 21.4741.00 29.65 N ATOM 2392 CA VAL C3080 14.237 11.135 21.542 1.00 28.33 CATOM 2393 CB VAL C3080 13.987 12.401 20.698 1.00 28.04 C ATOM 2394 CG1VAL C3080 12.497 12.701 20.643 1.00 27.55 C ATOM 2395 CG2 VAL C308014.739 13.576 21.289 1.00 27.56 C ATOM 2396 C VAL C3080 13.373 10.01421.007 1.00 28.05 C ATOM 2397 0 VAL C3080 13.518 9.600 19.858 1.00 27.43O ATOM 2398 N LEU C3081 12.482 9.513 21.853 1.00 27.62 N ATOM 2399 CALEU C3081 11.578 8.445 21.455 1.00 27.82 C ATOM 2400 CB LEU C3081 11.7247.235 22.391 1.00 27.48 C ATOM 2401 CG LEU C3081 13.107 6.575 22.5331.00 27.65 C ATOM 2402 CD1 LEU C3081 13.069 5.544 23.648 1.00 26.80 CATOM 2403 CG2 LEU C3081 13.534 5.928 21.223 1.00 26.81 C ATOM 2404 C LEUC3081 10.160 9.000 21.528 1.00 27.94 C ATOM 2405 0 LEU C3081 9.96510.194 21.744 1.00 27.66 O ATOM 2406 N ASN C3082 9.177 8.128 21.340 1.0028.22 N ATOM 2407 CA ASN C3082 7.775 8.523 21.400 1.00 28.52 C ATOM 2408CB ASN C3082 7.111 8.355 20.024 1.00 28.54 C ATOM 2409 CO ASN C30827.584 9.382 19.021 1.00 28.73 C ATOM 2410 001 ASN C3082 7.295 10.56919.148 1.00 29.62 O ATOM 2411 ND2 ASN C3082 8.321 8.932 18.020 1.0029.32 N ATOM 2412 C ASN C3082 7.053 7.647 22.422 1.00 28.28 C ATOM 2413O ASN C3082 7.199 6.421 22.407 1.00 28.06 O ATOM 2414 N ASN C3083 6.2808.274 23.308 1.00 27.85 N ATOM 2415 CA ASN C3083 5.537 7.520 24.304 1.0027.66 C ATOM 2416 CB ASM C3083 5.183 8.398 25.515 1.00 27.64 C ATOM 2417CG ASN C3083 4.203 9.527 25.189 1.00 27.67 C ATOM 2418 ODi ASN C30833.949 10.384 26.033 1.00 28.51 O ATOM 2419 ND2 ASN C3083 3.648 9.52723.986 1.00 27.19 N ATOM 2420 C ASN C3083 4.287 6.942 23.664 1.00 27.84C ATOM 2421 0 ASN C3083 3.988 7.233 22.501 1.00 27.10 O ATOM 2422 N GLUC3084 3.564 6.120 24.419 1.00 28.22 N ATOM 2423 CA GLU C3084 2.354 5.48323.910 1.00 28.64 C ATOM 2424 CB GLU C3084 1.655 4.679 25.018 1.00 29.96C ATOM 2425 CG GLU C3084 1.146 5.509 26.187 1.00 31.56 C ATOM 2426 CDGLU C3084 2.225 5.820 27.210 1.00 33.17 C ATOM 2427 OE1 GLU C3084 3.4045.994 26.821 1.00 33.53 O ATOM 2428 OE2 GLU C3084 1.888 5.903 28.4111.00 34.64 O ATOM 2429 C GLU C3084 1.367 6.471 23.291 1.00 28.20 C ATOM2430 0 GLU C3084 0.559 6.092 22.446 1.00 28.01 O ATOM 2431 N ARG C30851.435 7.734 23.702 1.00 27.98 N ATOM 2432 CA ARG C3085 0.526 8.74523.165 1.00 27.80 C ATOM 2433 CB ARG C3085 0.270 9.847 24.201 1.00 28.19C ATOM 2434 CG ARG C3085 −0.474 9.355 25.427 1.00 29.28 C ATOM 2435 CDARG C3085 −1.296 10.454 26.109 1.00 30.50 C ATOM 2436 NE ARG C3085−2.245 9.862 27.052 1.00 31.26 N ATOM 2437 CZ ARG C3085 −1.872 9.22128.153 1.00 32.48 C ATOM 2438 N 111 ARG C3085 −0.581 9.110 28.437 1.0033.70 N ATOM 2439 NH2 ARG C3085 −2.770 8.663 28.954 1.00 33.05 N ATOM2440 C ARG C3085 1.021 9.369 21.863 1.00 27.34 C ATOM 2441 0 ARG C30850.310 10.158 21.244 1.00 27.35 O ATOM 2442 N CL? C3086 2.237 9.01621.454 1.00 26.82 N ATOM 2443 CA GLY C3086 2.788 9.545 20.218 1.00 25.87C ATOM 2444 C GLY C3086 3.607 10.808 20.384 1.00 25.74 C ATOM 2445 0 GLYC3086 4.109 11.370 19.401 1.00 25.82 O ATOM 2446 N ALA C3087 3.75311.254 21.626 1.00 24.95 N ATOM 2447 CA ALA C3087 4.508 12.461 21.9201.00 24.57 C ATOM 2448 CB ALA C3087 3.933 13.147 23.155 1.00 24.64 CATOM 2449 C ALA C3087 5.991 12.183 22.130 1.00 24.46 C ATOM 2450 0 ALAC3087 6.372 11.277 22.878 1.00 24.54 O ATOM 2451 N PRO C3088 6.85112.964 21.461 1.00 24.09 N ATOM 2452 CD PRO C3088 6.501 14.011 20.4821.00 23.71 C ATOM 2453 CA PRO C3088 8.306 12.815 21.572 1.00 23.76 CATOM 2454 CB PRO C3088 8.825 13.714 20.451 1.00 23.93 C ATOM 2455 CG PROC3088 7.781 14.816 20.403 1.00 23.82 C ATOM 2456 C PRO C3088 8.79913.249 22.952 1.00 23.43 C ATOM 2457 0 PRO C3088 8.162 14.066 23.6101.00 23.03 O ATOM 2458 N TYR C3089 9.925 12.692 23.391 1.00 23.74 N ATOM2459 CA TYR C3089 10.496 13.028 24.698 1.00 24.43 C ATOM 2460 CB TYRC3089 9.671 −12.400 25.834 1.00 24.30 C ATOM 2461 CG TYR C3089 9.84310.904 25.973 1.00 24.64 C ATOM 2462 COl TYR C3089 10.832 10.363 26.8041.00 24.62 C ATOM 2463 CE1 TYR C3089 11.008 8.978 26.911 1.00 24.92 CATOM 2464 CG2 TYR C3089 9.033 10.027 25.256 1.00 24.84 C ATOM 2465 CB2TYR C3089 9.199 8.643 25.352 1.00 25.43 C ATOM 2466 CZ TYR C3089 10.1878.125 26.178 1.00 25.32 C ATOM 2467 OH TYR C3089 10.353 6.761 26.2361.00 25.52 O ATOM 2468 C TYR C3089 11.925 12.521 24.772 1.00 24.85 CATOM 2469 0 TYR C3089 12.279 11.552 24.103 1.00 25.10 O ATOM 2470 N PHEC3090 12.750 13.171 25.584 1.00 25.52 N ATOM 2471 CA PHE C3090 14.13512.742 25.714 1.00 26.19 C ATOM 2472 GB PHE C3090 15.038 13.901 26.1561.00 26.18 C ATOM 2473 CG PHE C3090 15.387 14.852 25.051 1.00 26.76 CATOM 2474 CD1 PHE C3090 14.541 15.912 24.725 1.00 27.13 C ATOM 2475 CG2PHE C3090 16.554 14.675 24.311 1.00 27.22 C ATOM 2476 CBl PHE C309014.851 16.792 23.675 1.00 27.19 C ATOM 2477 CB2 PHE C3090 16.882 15.54823.253 1.00 27.68 C ATOM 2478 CZ PHE C3090 16.025 16.608 22.936 1.0027.50 C ATOM 2479 C PHE C3090 14.277 11.595 26.693 1.00 26.31 C ATOM2480 0 PHE C3090 14.076 11.767 27.895 1.00 27.02 O ATOM 2481 N SER C309114.616 10.423 26.169 1.00 26.64 N ATOM 2482 CA SER C3091 14.818 9.23726.994 1.00 27.16 C ATOM 2483 GB SER C3091 14.549 7.964 26.185 1.0026.45 C ATOM 2484 OG SER C3091 15.280 7.970 24.974 1.00 27.09 O ATOM2485 C SER C3091 16.256 9.235 27.513 1.00 27.57 C ATOM 2486 0 SER C309116.594 8.485 28.424 1.00 27.76 O ATOM 2487 N GLN C3092 17.095 10.08626.928 1.00 28.18 N ATOM 2488 CA GLN C3092 18.490 10.199 27.340 1.0029.06 C ATOM 2489 GB GLN C3092 19.355 9.181 26.595 1.00 30.20 C ATOM2490 CG GLN C3092 20.843 9.363 26.840 1.00 31.72 C ATOM 2491 CD GLNC3092 21.280 8.873 28.211 1.00 32.79 C ATOM 2492 OE1 GLN C3092 21.3367.667 28.461 1.00 33.66 O ATOM 2493 NE2 GLN C3092 21.590 9.805 29.1051.00 33.12 N ATOM 2494 C GLN C3092 19.021 11.601 27.069 1.00 28.89 CATOM 2495 0 GLN C3092 18.889 12.118 25.954 1.00 29.04 O ATOM 2496 N ALAC3093 19.630 12.207 28.088 1.00 28.63 N ATOM 2497 CA ALA C3093 20.17913.556 27.963 1.00 28.35 C ATOM 2498 GB ALA C3093 19.040 14.565 27.8051.00 28.23 C ATOM 2499 C ALA C3093 21.047 13.945 29.159 1.00 28.01 CATOM 2500 0 ALA C3093 20.721 13.635 30.307 1.00 28.15 O ATOM 2501 N PROC3094 22.167 14.640 28.905 1.00 27.81 N ATOM 2502 CD PRO C3094 22.70215.035 27.590 1.00 27.69 C ATOM 2503 CA PRO C3094 23.066 15.067 29.9841.00 27.41 C ATOM 2504 GB PRO C3094 24.271 15.625 29.226 1.00 27.35 CATOM 2505 CG PRO C3094 23.658 16.148 27.960 1.00 27.34 C ATOM 2506 C PROC3094 22.409 16.108 30.883 1.00 27.24 C ATOM 2507 0 PRO C3094 22.99217.150 31.172 1.00 27.73 O ATOM 2508 N PHE C3095 21.195 15.820 31.3301.00 26.89 N ATOM 2509 CA PHE . C3095 20.457 16.740 32.182 1.00 26.88 CATOM 2510 GB PHE C3095 19.603 17.680 31.314 1.00 26.34 C ATOM 2511 COPHE C3095 18.986 18.820 32.081 1.00 25.69 C ATOM 2512 COl PHE C309519.789 19.707 32.796 1.00 24.82 C ATOM 2513 CG2 PHE C3095 17.606 18.97332.133 1.00 24.80 C ATOM 2514 GEl PHE C3095 19.224 20.722 33.556 1.0024.83 C ATOM 2515 CB2 PHE C3095 17.031 19.985 32.890 1.00 24.99 C ATOM2516 CZ PHE C3095 17.841 20.862 33.605 1.00 24.98 C ATOM 2517 C PHEG3095 19.569 15.927 33.115 1.00 27.25 C ATOM 2518 0 PHE C3095 18.92414.983 32.684 1.00 28.50 O ATOM 2519 N SER C3096 19.525 16.284 34.3901.00 27.37 N ATOM 2520 CA SER C3096 18.710 15.530 35.332 1.00 27.95 CATOM 2521 GB SER C3096 19.542 15.174 36.565 1.00 28.67 C ATOM 2522 00SER C3096 20.425 16.230 36.883 1.00 30.49 O ATOM 2523 C SER C3096 17.40316.202 35.754 1.00 27.66 C ATOM 2524 0 SER C3096 16.663 15.665 36.5771.00 27.25 O ATOM 2525 N GLY C3097 17.117 17.372 35.192 1.00 26.91 NATOM 2526 CA GLY C3097 15.874 18.045 35.521 1.00 26.05 C ATOM 2527 C GLYC3097 14.839 17.654 34.488 1.00 25.55 C ATOM 2528 0 GLY C3097 15.04716.696 33.745 1.00 25.35 O ATOM 2529 N LYS C3098 13.729 18.384 34.4281.00 25.19 N ATOM 2530 CA LYS C3098 12.690 18.086 33.452 1.00 24.30 CATOM 2531 CB LYS C3098 11.820 18.543 33.945 1.00 24.76 C ATOM 2532 CGLYS C3098 10.863 17.934 35.237 1.00 25.27 C ATOM 2533 CD LYS C3098 9.39718.241 35.459 1.00 26.28 C ATOM 2534 CB LYS C3098 8.973 17.880 36.8601.00 26.82 C ATOM 2535 NZ LYS C3098 9.334 16.468 37.155 1.00 28.61 NATOM 2536 G LYS C3098 12.978 18.774 32.119 1.00 23.93 C ATOM 2537 0 LYSC3098 13.330 19.954 32.077 1.00 23.38 O ATOM 2538 N ILE C3099 12.82118.019 31.034 1.00 23.34 N ATOM 2539 CA ILE C3099 13.033 18.536 29.6901.00 22.75 C ATOM 2540 CB ILE C3099 13.960 17.613 28.874 1.00 22.58 CATOM 2541 CG2 ILE C3099 14.345 18.292 27.558 1.00 22.52 C ATOM 2542 CG1ILE C3099 15.219 17.291 29.688 1.00 22.55 C ATOM 2543 COl ILE C309916.199 16.357 28.985 1.00 22.28 C ATOM 2544 C ILE C3099 11.676 18.61728.990 1.00 22.48 C ATOM 2545 0 ILE C3099 11.054 17.591 28.699 1.0022.47 O ATOM 2546 N TRP C3100 11.205 19.835 28.743 1.00 21.77 N ATOM2547 CA TRP C3100 9.926 20.008 28.071 1.00 20.54 C ATOM 2548 CB TRPC3100 9.180 21.228 28.600 1.00 19.83 C ATOM 2549 CG TRP C3100 8.90021.139 30.066 1.00 19.91 C ATOM 2550 CG2 TRP C3100 7.806 20.455 30.6941.00 19.80 C ATOM 2551 CB2 TRP C3100 7.968 20.605 32.091 1.00 19.84 CATOM 2552 CB3 TRP C3100 6.704 19.727 30.211 1.00 19.87 C ATOM 2553 COlTRP C3100 9.660 21.660 31.081 1.00 19.93 C ATOM 2554 NEl TRP C3100 9.10621.343 32.296 1.00 19.91 N ATOM 2555 CZ2 TRP C3100 7.069 20.058 33.0151.00 19.27 C ATOM 2556 CZ3 TRP C3100 5.808 19.181 31.128 1.00 19.78 CATOM 2557 CH2 TRP C3100 6.000 19.352 32.520 1.00 20.41 C ATOM 2558 C TRPC3100 10.239 20.174 26.611 1.00 20.42 C ATOM 2559 0 TRP C3100 10.83121.174 26.195 1.00 21.30 O ATOM 2560 N LEU C3101 9.845 19.173 25.8381.00 19.69 N ATOM 2561 CA LEU C3101 10.097 19.143 24.416 1.00 19.35 CATOM 2562 CB LEU C3101 10.903 17.891 24.072 1.00 18.36 C ATOM 2563 CGLEU C3101 10.885 17.499 22.592 1.00 18.24 C ATOM 2564 CD1 LEU C310111.677 18.536 21.786 1.00 16.55 C ATOM 2565 CG2 LEU C3101 11.466 16.09722.414 1.00 17.56 C ATOM 2566 CLEt) C3101 8.831 19.145 23.587 1.00 19.41C ATOM 2567 0 LEU C3101 7.846 18.493 23.929 1.00 19.45 O ATOM 2568 N SERC3102 8.860 19.885 22.490 1.00 19.43 N ATOM 2569 CA SER C3102 7.72219.899 21.596 1.00 19.85 C ATOM 2570 CB SER C3102 6.793 21.082 21.8731.00 19.85 C ATOM 2571 OG SER C3102 5.550 20.887 21.212 1.00 19.01 OATOM 2572 C SER C3102 8.269 19.972 20.190 1.00 20.13 C ATOM 2573 0 SERC3102 9.272 20.637 19.939 1.00 19.67 O ATOM 2574 N ILE C3103 7.62419.251 19.282 1.00 21.04 N ATOM 2575 CA ILE C3103 8.037 19.231 17.8891.00 22.10 C ATOM 2576 CB ILE C3103 8.735 17.906 17.523 1.00 21.92 CATOM 2577 CG2 ILE C3103 9.127 17.922 16.059 1.00 21.89 C ATOM 2578 CG1ILE C3103 9.963 17.681 18.405 1.00 22.24 C ATOM 2579 CD1 ILE C310310.695 16.376 18.094 1.00 22.36 C ATOM 2580 C ILE C3103 6.804 19.34617.010 1.00 23.17 C ATOM 2581 0 ILE C3103 5.753 18.805 17.338 1.00 23.73O ATOM 2582 N SER C3104 6.932 20.051 15.896 1.00 23.79 N ATOM 2583 CASER C3104 5.829 20.186 14.965 1.00 24.82 C ATOM 2584 CB SER C3104 4.98921.419 15.294 1.00 24.69 C ATOM 2585 OG SER C3104 3.905 21.546 14.3901.00 24.65 O ATOM 2586 C SER c3104 6.428 20.295 13.567 1.00 25.82 C ATOM2587 0 SER C3104 7.577 20.690 13.403 1.00 25.83 O ATOM 2588 N HIS C31055.646 19.929 12.560 1.00 27.14 N. ATOM 2589 CA HIS C3105 6.140 19.99611.200 1.00 28.67 C ATOM 2590 CB HIS C3105 6.841 18.686 10.819 1.0030.20 C ATOM 2591 CG HIS C3105 5.901 17.542 10.584 1.00 31.48 C ATOM2592 CG2 HIS C3105 5.474 16.961 9.437 1.00 32.52 C ATOM 2593 ND1 HISC3105 5.252 16.887 11.607 1.00 33.00 N ATOM 2594 CBl HIS C3105 4.46515.952 11.103 1.00 33.08 C ATOM 2595 NE2 HIS C3105 4.580 15.977 9.7871.00 33.14 N ATOM 2596 C HIS C3105 5.046 20.253 10.187 1.00 29.03 C ATOM2597 0 HIS C3105 3.862 20.082 10.468 1.00 28.87 O ATOM 2598 N THR C31065.478 20.682 9.009 1.00 29.70 N ATOM 2599 CA THR C3106 4.609 20.9187.871 1.00 30.87 C ATOM 2600 CB THR C3106 4.542 22.416 7.492 1.00 30.95C ATOM 2601 OGi THR C3106 5.853 22.895 7.185 1.00 31.53 O ATOM 2602 CG2THR C3106 3.970 23.231 8.631 1.00 31.66 C ATOM 2603 C THR C3106 5.31020.118 6.758 1.00 31.46 C ATOM 2604 0 THR C3106 6.288 19.411 7.032 1.0031.17 O ATOM 2605 N ASP C3107 4.834 20.223 5.521 1.00 32.04 N ATOM 2606CA ASP C3107 5.444 19.475 4.423 1.00 32.74 C ATOM 2607 CD ASP C31074.584 19.570 3.151 1.00 33.89 C ATOM 2608 CG ASP C3107 3.252 18.8363.276 1.00 35.29 C ATOM 2609 ODi ASP C3107 3.059 18.077 4.257 1.00 35.09O ATOM 2610 002 ASP C3107 2.396 19.017 2.379 1.00 35.84 O ATOM 2611 CASP C3107 6.861 19.942 4.096 1.00 32.51 C ATOM 2612 0 ASP C3107 7.68019.158 3.609 1.00 32.63 O ATOM 2613 NGL~I C3108 7.152 21.210 4.371 1.0031.99 N ATOM 2614 CA GLN C3108 8.467 21.768 4.068 1.00 31.59 C ATOM 2615CR GLN C3108 8.310 23.119 3.362 1.00 32.00 C ATOM 2616 CG GLN C31087.482 23.077 2.086 1.00 32.40 ATOM 2617 CD GLN C3108 7.294 24.452 1.4690.05 32.28 C ATOM 2618 OE1 GLN C3108 6.650 24.597 0.430 0.05 32.30 OATOM 2619 NE2 GLN C3108 7.856 25.469 2.110 0.05 32.28 N ATOM 2620 C GLNC3108 9.391 21.957 5.272 1.00 30.94 C ATOM 2621 0 GLN C3108 10.61021.833 5.145 1.00 30.85 O ATOM 2622 N PHE . C3109 8.822 22.258 6.4361.00 30.12 N ATOM 2623 CA PHE C3109 9.648 22.489 7.610 1.00 29.07 C ATOM2624 CB PHE C3109 9.652 23.980 7.953 1.00 29.62 C ATOM 2625 CG PHE C310910.111 24.857 6.827 1.00 30.64 C ATOM 2626 COl PHE C3109 9.215 25.2755.845 1.00 31.09 C ATOM 2627 CG2 PHE C3109 11.440 25.259 6.738 1.0030.59 C ATOM 2628 CBl PHE C3109 9.636 26.084 4.788 1.00 31.21 C ATOM2629 CB2 PHE C3109 11.870 26.066 5.688 1.00 30.89 C ATOM 2630 CZ PHEC3109 10.964 26.480 4.709 1.00 31.08 C ATOM 2631 C PHE C3109 9.29221.716 8.860 1.00 28.01 C ATOM 2632 0 PHE C3109 8.252 21.065 8.936 1.0028.14 O ATOM 2633 N VAL C3110 10.192 21.798 9.838 1.00 26.84 N ATOM 2634CA VAL C3110 10.019 21.175 11.140 1.00 25.60 C ATOM 2635 CB VAL C311010.766 19.822 11.250 1.00 25.63 C ATOM 2636 CG1 VAL C3110 12.268 20.03511.191 1.00 25.54 C ATOM 2637 CG2 VAL C3110 10.387 19.133 12.554 1.0025.58 C ATOM 2638 C VAL C3110 10.580 22.139 12.187 1.00 24.84 C ATOM2639 0 VAL C3110 11.596 22.798 11.957 1.00 24.75 O ATOM 2640 N THR C31119.911 22.239 13.328 1.00 23.62 N ATOM 2641 CA THR C3111 10.377 23.12014.395 1.00 23.00 C ATOM 2642 CB THR C3111 9.451 24.332 14.583 1.0023.10 C ATOM 2643 OGi THR C3111 8.138 23.871 14.924 1.00 24.21 O ATOM2644 CG2 THR C3111 9.369 25.145 13.306 1.00 23.43 C ATOM 2645 C THRC3111 10.424 22.363 15.712 1.00 22.01 C ATOM 2646 0 THR C3111 9.61621.466 15.951 1.00 22.10 O ATOM 2647 N ALA C3122 11.382 22.726 16.5541.00 21.05 N ATOM 2648 CA ALA C3112 11.532 22.110 17.859 1.00 20.79 CATOM 2649 CB ALA C3112 12.710 21.135 17.846 1.00 20.00 C ATOM 2650 C ALAC3112 11.741 23.194 18.927 1.00 20.81 C ATOM 2651 0 ALA C3112 12.36724.216 18.672 1.00 20.76 O ATOM 2652 N SER C3113 11.199 22.968 20.1181.00 20.90 N ATOM 2653 CA SER C3113 11.346 23.909 21.215 1.00 20.61 CATOM 2654 CB SER C3113 10.061 24.721 21.413 1.00 20.72 C ATOM 2655 OGSER C3113 10.176 25.598 22.526 1.00 20.34 O ATOM 2656 C SER C3113 11.65323.128 22.477 1.00 20.63 C ATOM 2657 0 SER C3113 11.013 22.119 22.7591.00 20.86 O ATOM 2658 N VAL C3114 12.633 23.599 23.237 1.00 20.54 NATOM 2659 CA VAL C3114 13.019 22.938 24.463 1.00 20.40 C ATOM 2660 CBVAL C3114 14.349 22.188 24.288 1.00 20.41 C ATOM 2661 COl VAL C311414.872 21.743 25.647 1.00 19.44 C ATOM 2662 CG2 VAL C3114 14.148 20.97623.357 1.00 20.11 C ATOM 2663 C VAL C3114 13.159 23.883 25.644 1.0020.99 C ATOM 2664 0 VAL C3114 13.804 24.938 25.552 1.00 20.99 O ATOM2665 N ILE C3115 12.543 23.494 26.756 1.00 21.35 N ATOM 2666 CA ILEC3115 12.626 24.269 27.980 1.00 22.44 C ATOM 2667 CB ILE C3115 11.25024.816 28.428 1.00 22.27 C ATOM 2668 CG2 ILE C3115 11.440 25.821 29.5621.00 22.27 C ATOM 2669 CG1 ILE C3115 10.553 25.529 27.262 1.00 22.90 CATOM 2670 COl ILE C3115 9.141 25.990 27.562 1.00 22.49 C ATOM 2671 C ILEC3115 13.167 23.360 29.077 1.00 23.09 C ATOM 2672 0 ILE C3115 12.57022.331 29.388 1.00 23.11 O ATOM 2673 N LEU C3116 14.311 23.730 29.6401.00 23.90 N ATOM 2674 CA LEU C3116 14.912 22.959 30.720 1.00 25.63 CATOM 2675 CB LEU C3116 16.434 23.051 30.667 1.00 24.96 C ATOM 2676 CGLEU C3116 17.007 22.497 29.366 1.00 24.50 C ATOM 2677 COl LEU C311618.508 22.663 29.350 1.00 23.62 C ATOM 2678 CG2 LEU C3116 16.596 21.02929.236 1.00 24.58 C ATOM 2679 C LEU C3116 14.418 23.524 32.036 1.0027.20 C ATOM 2680 0 LEU C3116 14.412 24.743 32.236 1.00 27.34 O ATOM2681 N GLU C3117 13.998 22.636 32.930 1.00 28.70 N ATOM 2682 CA GLUC3117 13.490 23.061 34.226 1.00 30.61 C ATOM 2683 CB GLU C3117 11.95722.951 34.249 1.00 30.11 C ATOM 2684 CG GLU C3117 11.322 23.257 35.5921.00 30.29 C ATOM 2685 CD GLU C3117 9.808 23.100 35.585 1.00 30.63 CATOM 2686 QEl GLU C3117 9.313 22.085 35.043 1.00 30.65 O ATOM 2687 OE2GLU C3117 9.114 23.985 36.133 1.00 30.59 O ATOM 2688 C GLU C3117 14.08922.241 35.357 1.00 31.98 C ATOM 2689 0 GLU C3117 14.353 21.052 35.2051.00 32.46 O ATOM 2690 N GLU C3118 14.321 22.900 36.485 1.00 33.79 NATOM 2691 CA GLU C3118 24.863 22.257 37.674 1.00 35.41 C ATOM 2692 CBGLU C3118 16.264 22.779 37.990 1.00 36.58 C ATOM 2693 CG GLU C311817.396 21.983 37.366 1.00 38.74 C ATOM 2694 CD GLU C3118 17.335 20.50737.733 1.00 40.59 C ATOM 2695 OE1 GLU C3118 16.936 20.189 38.881 1.0041.34 O ATOM 2696 OE2 GLU C3118 17.700 19.669 36.877 1.00 41.36 O ATOM2697 C GLU C3118 13.940 22.578 38.837 1.00 36.11 C ATOM 2698 O GLU C311813.351 21.632 39.403 1.00 37.15 O ATOM 2699 OXT GLU C3118 13.813 23.77839.156 1.00 36.00 O TER 2700 GLU C3118 ATOM 2701 O HOH W  1 8.576 28.00319.046 1.00 26.06 O ATOM 2702 O HOH W  2 11.001 13.668 14.737 1.00 16.99O ATOM 2703 O HOH W  3 −5.347 33.382 14.724 1.00 27.55 O ATOM 2704 O HOHW  4 19.615 31.388 19.825 1.00 18.58 O ATOM 2705 O HOH W  5 −11.21636.113 18.617 1.00 38.18 O ATOM 2706 O HOH W  6 0.159 37.746 18.293 1.0026.61 O ATOM 2707 O HOH W  7 1.276 36.190 20.543 1.00 28.54 O ATOM 2708O HOH W  8 12.334 34.067 2.484 1.00 24.27 O ATOM 2709 O HOH W  9 0.2556.277 33.704 1.00 25.24 O ATOM 2710 O HOH W 1O 18.182 37.167 27.027 1.0023.05 O ATOM 2711 O HOH W 11 −4.577 31.410 31.511 1.00 38.36 O ATOM 2712O HOH W 12 −1.511 45.557 32.920 1.00 53.67 O ATOM 2713 O HOH W 13 18.44825.653 12.095 1.00 26.48 O ATOM 2714 O HOH W 14 3.912 2.648 29.570 1.0020.27 O ATOM 2715 O HOH W 15 −11.595 44.974 29.760 1.00 29.90 O ATOM2716 O HOH W 16 25.183 18.367 31.463 1.00 31.92 O ATOM 2717 O HOH W 171.272 28.443 2.735 1.00 24.74 O ATOM 2718 O HOH W 18 19.674 51.864 7.5421.00 32.28 O ATOM 2719 O HOH W 19 7.406 44.679 0.671 1.00 37.76 O ATOM2720 O HOH W 20 9.102 25.639 41.587 1.00 37.75 O ATOM 2721 O HOH W 21−2.117 42.358 29.367 1.00 23.51 O ATOM 2722 O HOH W 22 12.144 15.09131.453 1.00 40.21 O ATOM 2723 O HOH W 23 20.216 37.895 14.318 1.00 23.27O ATOM 2724 O HOH W 24 15.409 30.644 36.448 1.00 34.67 O ATOM 2725 O HOHW 25 8.888 28.186 21.855 1.00 19.15 O ATOM 2726 O HOH W 26 −6.604 42.28129.309 1.00 52.83 O ATOM 2727 O HOH W 27 20.104 53.238 15.360 1.00 42.16O ATOM 2728 O HOH W 28 24.519 36.311 10.567 1.00 45.76 O ATOM 2729 O HOHW 29 17.712 23.831 7.356 1.00 49.27 O ATOM 2730 O HOH W 30 −6.885 28.65132.939 1.00 45.10 O ATOM 2731 O HOH W 31 −4.869 16.926 12.390 1.00 39.22O ATOM 2732 O HOH W 32 20.935 28.085 34.073 1.00 42.57 O ATOM 2733 O HOHW 33 21.868 15.456 38.834 1.00 28.55 O ATOM 2734 O HOH W 34 30.17127.602 20.593 1.00 34.40 O ATOM 2735 O HOH W 35 20.651 33.038 6.426 1.0038.43 O ATOM 2736 O HOH W 36 10.238 19.208 1.078 1.00 45.56 O ATOM 2737O HOH W 37 13.283 54.499 28.613 1.00 29.72 O ATOM 2738 O HOH W 38−11.211 32.999 2.256 1.00 31.79 O ATOM 2739 O HOH W 39 9.887 29.79836.670 1.00 39.85 O ATOM 2740 O HOH W 40 18.546 10.765 31.009 1.00 38.20O ATOM 2741 O HOH W 41 24.510 24.190 30.902 1.00 36.49 O ATOM 2742 O HOHW 42 30.384 38.300 20.406 1.00 44.88 O ATOM 2743 O HOH W 43 18.88528.685 22.975 1.00 28.61 O ATOM 2744 O HOH W 44 2.917 33.308 36.961 1.0038.63 O ATOM 2745 O HOH W 45 20.025 .37.807 29.500 1.00 35.61 O ATOM2746 O HOH W 46 8.253 16.151 27.102 1.00 45.55 O ATOM 2747 O HOH W 477.572 21.032 36.495 1.00 16.73 O ATOM 2748 O HOH W 48 19.451 28.61127.413 1.00 35.89 O ATOM 2749 O HOH W 49 11.476 8.815 36.574 1.00 25.09O ATOM 2750 O HOH W 50 14.236 27.513 3.754 1.00 34.47 O ATOM 2751 O HOHW 51 5.103 9.140 28.941 1.00 41.40 O ATOM 2752 O HOH W 52 34.054 32.83425.976 1.00 45.36 O ATOM 2753 O HOH W 53 12.068 21.222 2.790 1.00 39.74O ATOM 2754 O HOH W 54 2.919 30.077 39.125 1.00 41.17 O ATOM 2755 O HOHW 55 27.605 12.175 17.892 1.00 50.62 O ATOM 2756 O HOH W 56 −12.86826.916 30.495 1.00 43.36 O ATOM 2757 O HOH W 57 9.027 13.611 36.816 1.0043.33 O ATOM 2758 O HOH W 58 7.507 37.992 7.686 1.00 29.16 O ATOM 2759 OHOH W 59 18.024 26.076 4.943 1.00 45.92 O ATOM 2760 O HOH W 60 21.88953.044 19.501 1.00 41.90 O ATOM 2761 O HOH W 61 34.566 32.372 30.6921.00 50.00 O ATOM 2762 O HOH W 62 5.289 23.268 4.539 1.00 26.10 O ATOM2763 O HOH W 63 21.724 28.905 29.036 1.00 54.44 O ATOM 2764 O HOH W 647.000 28.471 37.399 1.00 36.37 O ATOM 2765 O HOH W 65 31.382 30.72521.632 1.00 32.29 O ATOM 2766 O HOH W 66 28.182 46.827 4.332 1.00 48.39O ATOM 2767 O HOH W 67 7.410 9.794 14.247 1.00 49.84 O ATOM 2768 O HOHW 68 31.517 25.424 22.117 1.00 43.26 O ATOM 2769 O HOH W 69 −5.30133.373 34.239 1.00 34.98 O ATOM 2770 O HOH W 70 36.871 33.074 30.2811.00 41.21 O ATOM 2771 O HOH W 71 24.903 41.702 17.966 1.00 33.98 O ATOM2772 O HOH W 72 17.963 38.386 31.211 1.00 35.46 O ATOM 2773 O HOH W 7320.723 48.845 4.797 1.00 50.12 O ATOM 2774 O HOH W 74 −8.379 30.15931.227 1.00 58.73 O ATOM 2775 O HOH W 75 −1.343 19.609 10.013 1.00 53.09O ATOM 2776 O HOH W 76 15.642 12.801 31.165 1.00 65.31 O ATOM 2777 O HOHW 77 −14.605 25.461 6.171 1.00 36.87 O ATOM 2778 O HOH W 78 8.718 39.5940.632 1.00 44.46 O ATOM 2779 O HOH W 79 22.426 26.766 11.895 1.00 39.57O ATOM 2780 O HOH W 80 1.403 12.128 29.940 1.00 41.04 O ATOM 2781 O HOHW 81 9.724 26.576 37.441 1.00 52.28 O ATOM 2782 O HOH W 82 −20.85235.093 18.162 1.00 32.23 O ATOM 2783 O HOH W 83 −22.727 33.513 17.1601.00 46.00 O ATOM 2784 O HOH W 84 −9.764 38.910 4.301 1.00 38.92 O ATOM2785 O HOH W 85 4.067 40.345 32.364 1.00 54.10 O ATOM 2786 O HOH W 868.783 44.044 3.423 1.00 45.06 O ATOM 2787 O HOH W 87 19.259 34.58726.113 1.00 34.60 O ATOM 2788 O HOH W 88 19.168 34.051 31.232 1.00 40.61O ATOM 2789 O HOH W 89 −17.637 26.480 8.650 1.00 35.76 O ATOM 2790 O HOHW 90 5.883 33.114 4.115 1.00 36.72 O ATOM 2791 O HOH W 91 5.401 9.2713.439 1.00 23.12 O ATOM 2792 O HOH W 92 16.578 55.625 9.782 1.00 34.03 OATOM 2793 O HOH W 93 −6.649 22.603 36.177 1.00 49.27 O ATOM 2794 O HOHW 94 12.263 32.477 39.013 1.00 44.31 O ATOM 2795 O HOH W 95 11.06451.183 10.359 1.00 46.81 O ATOM 2796 O HOH W 96 −16.103 28.570 5.9991.00 45.48 O ATOM 2797 O HOH W 97 19.096 56.580 8.669 1.00 48.52 O ATOM2798 O HOH W 98 −0.441 38.083 25.842 1.00 30.49 O ATOM 2799 O HOH W 9918.821 50.159 23.847 1.00 35.93 O ATOM 2800 O HOH W 100 21.593 29.43922.517 1.00 46.08 O ATOM 2801 O HOH W 101 24.154 31.033 26.613 1.0041.03 O ATOM 2802 O HOH W 102 18.634 43.303 30.404 1.00 40.85 O ATOM2803 O HOH W 103 19.981 32.247 35.107 1.00 36.43 O ATOM 2804 O HOH W 104−10.088 29.062 1.003 1.00 36.43 O ATOM 2805 O HOH W 105 −18.529 19.6315.334 1.00 38.77 O ATOM 2806 O HOH W 106 −20.984 28.385 15.095 1.0040.22 O ATOM 2807 O HOH W 107 −19.013 26.762 15.815 1.00 32.06 O ATOM2808 O HOH W 108 −14.266 19.001 19.100 1.00 41.92 O ATOM 2809 O HOHW 109 7.301 10.6941 1.123 1.00 37.73 O ATOM 2810 O HOH W 110 24.39818.549 24.386 1.00 37.13 O ATOM 2811 O HOH W 111 2.259 41.877 17.6031.00 33.35 O ATOM 2812 O HOH W 112 22.143 19.952 8.110 1.00 46.84 O ATOM2813 O HOH W 113 −4.490 20.867 8.897 1.00 50.63 O ATOM 2814 O HOH W 1140.274 4.462 29.620 1.00 46.55 O ATOM 2815 O HOH W 115 9.966 5.205 19.8791.00 29.38 O ATOM 2816 O HOH W 116 11.609 14.420 39.214 1.00 45.17 OATOM 2817 O HOH W 117 21.720 11.206 36.139 1.00 23.23 O ATOM 2818 O HOHW 118 21.825 46.932 3.417 1.00 42.90 O ATOM 2819 O HOH W 119 0.06730.700 1.199 1.00 54.52 O ATOM 2820 O HOH W 120 10.218 22.583 38.8061.00 43.46 O ATOM 2821 O HOH W 121 0.686 27.966 42.608 1.00 42.57 O ATOM2822 O HOH W 122 23.786 35.976 16.687 1.00 27.98 O ATOM 2823 O HOH W 12325.685 36.926 14.983 1.00 35.19 O ATOM 2824 O HOH W 124 5.593 17.61520.205 1.00 22.22 O ATOM 2825 O HOH W 125 −3.621 36.444 16.059 1.0038.53 O ATOM 2826 O HOH W 126 −6.822 38.370 14.785 1.00 35.77 O ATOM2827 O HOH W 127 8.658 28.063 15.129 1.00 32.14 O ATOM 2828 O HOH W 128−4.302 30.987 36.514 1.00 38.06 O ATOM 2829 O HOH W 129 −1.650 29.06838.757 1.00 30.65 O TER 2830 HOH W 129 END

[0362] TABLE 4 REMARK coordinates from restrained individual B-factorrefinement REMARK refinement resolution: 500.0 − 2.05 A REMARK startingr = 0.2078  free_r = 0.2459 REMARK final r = 0.2076  free_r = 0.2466REMARK B rmsd for bonded mainchain atoms = 1.338  target = 1.5 REMARK Brmsd for bonded sidechain atoms = 2.017  target = 2.0 REMARK B rmsd forangle mainchain atoms = 2.137  target = 2.0 REMARK B rmsd for anglesidechain atoms = 3.077  target = 2.5 REMARK wa = 1.98578 REMARK rweight= 0.12477 REMARK target = mlf · steps = 30 REMARK sg = C2  a =116.043  b = 59.291  c = 49.629 alpha = 90  beta = 98.768  gamma = 90REMARK parameter file 1  CNX_TOPPAR:protein_rep.param REMARK parameterfile 2  CNX_TOPPAR:water_rep.param REMARK parameter file3  CNX_TOPPAR:ion.param REMARK molecular structure file: generate.psfREMARK input coordinates: minimize.pdb REMARK reflection file =../data/x-ray_data.cv REMARK ncs = none REMARK B-correction resolution:6.0 − 2.05 REMARK initial B-factor correction applied to fobs:REMARK  B11 = 0.091  B22 = −2.051  B33 = 1.959 REMARK  B12 = 0.000  B13= 0.271  B23 = 0.000 REMARK B-factor correction applied to coordinatearray B: −0.022 REMARK bulk solvent: (Mask) density level = 0.368883e/A{circumflex over ( )}3, B-factor = 52.2583 A{circumflex over ( )}2REMARK reflections with |Fobs|/sigma_F < 0.0 rejected REMARK reflectionswith |Fobs| > 10000 * rms (Fobs) rejected REMARK theoretical totalnumber of refl. in resol. range: 21048 (100.0%) REMARK number ofunobserved reflections (no entry or |F| = 0): 1611 (7.7%) REMARK numberof reflections rejected: 0 (0.0%) REMARK total number of reflectionsused: 19437 (92.3%) REMARK number of reflections in working set: 18494(87.9%) REMARK number of reflections in test set: 943 (4.5%) REMARKFILENAME = “acps_native 2.pdb”: created by user: rx83663 REMARK Writtenby CNX VERSION: 2000 ATOM 1 CB MET A1003 36.109 5.413 19.351 1.00 32.48C ATOM 2 CG MET A1003 35.473 5.856 20.649 1.00 37.79 C ATOM 3 SD META1003 36.607 6.848 21.649 1.00 45.89 S ATOM 4 CE MET A1003 36.791 8.31420.599 1.00 43.10 C ATOM 5 C MET A1003 33.900 5.073 18.225 1.00 27.65 CATOM 6 O MET A1003 33.795 6.027 17.463 1.00 25.93 O ATOM 7 N MET A100335.971 4.133 17.240 1.00 28.87 N ATOM 8 CA MET A1003 35.262 4.452 18.5151.00 29.37 C ATOM 9 N ILE A1004 32.860 4.513 18.832 1.00 27.12 N ATOM 10CA ILE A1004 31.500 5.005 18.649 1.00 25.95 C ATOM 11 CB ILE A100430.463 3.928 19.020 1.00 25.43 C ATOM 12 CG2 ILE A1004 29.048 4.51618.954 1.00 24.89 C ATOM 13 CG1 ILE A1004 30.604 2.730 18.076 1.00 24.55C ATOM 14 CD1 ILE A1004 29.619 1.616 18.347 1.00 26.14 C ATOM 15 C ILEA1004 31.289 6.214 19.546 1.00 27.18 C ATOM 16 O ILE A1004 31.700 6.21220.703 1.00 27.39 O ATOM 17 N VAL A1005 30.655 7.251 19.018 1.00 24.87 NATOM 18 CA VAL A1005 30.420 8.439 19.818 1.00 25.40 C ATOM 19 CB VALA1005 31.326 9.589 19.346 1.00 26.42 C ATOM 20 CG1 VAL A1005 32.7819.240 19.648 1.00 26.20 C ATOM 21 CG2 VAL A1005 31.153 9.818 17.860 1.0027.65 C ATOM 22 C VAL A1005 28.955 8.857 19.794 1.00 24.30 C ATOM 23 OVAL A1005 28.592 9.964 20.195 1.00 23.88 O ATOM 24 N GLY A1006 28.1027.952 19.331 1.00 23.00 N ATOM 25 CA GLY A1006 26.687 8.261 19.290 1.0019.45 C ATOM 26 C GLY A1006 25.887 7.300 18.443 1.00 18.59 C ATOM 27 OGLY A1006 26.396 6.730 17.480 1.00 16.47 O ATOM 28 N HIS A1007 24.6217.130 18.809 1.00 16.39 N ATOM 29 CA HIS A1007 23.720 6.249 18.092 1.0015.38 C ATOM 30 CB HIS A1007 23.825 4.818 18.636 1.00 17.15 C ATOM 31 CGHIS A1007 22.877 3.853 17.993 1.00 18.41 C ATOM 32 CD2 HIS A1007 22.0752.902 18.528 1.00 17.85 C ATOM 33 ND1 HIS A1007 22.690 3.789 16.628 1.0017.93 N ATOM 34 CE1 HIS A1007 21.811 2.841 16.351 1.00 19.72 C ATOM 35NE2 HIS A1007 21.423 2.288 17.486 1.00 18.78 N ATOM 36 C HIS A100722.302 6.768 18.262 1.00 16.54 C ATOM 37 O HIS A1007 21.883 7.113 19.3641.00 15.23 O ATOM 38 N GLY A1008 21.568 6.844 17.162 1.00 13.65 N ATOM39 CA GLY A1008 20.204 7.303 17.250 1.00 14.59 C ATOM 40 C GLY A100819.364 6.591 16.220 1.00 16.81 C ATOM 41 O GLY A1008 19.864 6.208 15.1541.00 14.95 O ATOM 42 N ILE A1009 18.089 6.394 16.538 1.00 16.05 N ATOM43 CA ILE A1009 17.186 5.750 15.603 1.00 16.53 C ATOM 44 CB ILE A100916.841 4.297 16.012 1.00 16.37 C ATOM 45 CG2 ILE A1009 18.087 3.43615.974 1.00 15.97 C ATOM 46 CG1 ILE A1009 16.168 4.284 17.393 1.00 14.54C ATOM 47 CD1 ILE A1009 15.697 2.907 17.831 1.00 15.26 C ATOM 48 C ILEA1009 15.898 6.541 15.578 1.00 18.21 C ATOM 49 O ILE A1009 15.681 7.42316.408 1.00 18.91 O ATOM 50 N ASP A1010 15.041 6.218 14.623 1.00 19.48 NATOM 51 CA ASP A1010 13.759 6.880 14.520 1.00 20.47 C ATOM 52 CB ASPA1010 13.930 8.295 13.969 1.00 21.20 C ATOM 53 CG ASP A1010 12.614 9.01313.813 1.00 24.68 C ATOM 54 OD1 ASP A1010 12.002 8.901 12.725 1.00 25.58O ATOM 55 OD2 ASP A1010 12.182 9.675 14.785 1.00 21.51 O ATOM 56 C ASPA1010 12.822 6.094 13.630 1.00 22.13 C ATOM 57 O ASP A1010 13.249 5.48512.641 1.00 21.63 O ATOM 58 N ILE A1011 11.548 6.074 14.011 1.00 20.69 NATOM 59 CA ILE A1011 10.525 5.403 13.226 1.00 22.73 C ATOM 60 CB ILEA1011 10.019 4.103 13.903 1.00 22.88 C ATOM 61 CG2 ILE A1011 9.505 4.39815.320 1.00 23.25 C ATOM 62 CG1 ILE A1011 8.922 3.476 13.033 1.00 24.40C ATOM 63 CD1 ILE A1011 8.496 2.096 13.466 1.00 25.25 C ATOM 64 C ILEA1011 9.394 6.412 13.094 1.00 23.63 C ATOM 65 O ILE A1011 9.016 7.06114.071 1.00 23.36 O ATOM 66 N GLU A1012 8.869 6.549 11.882 1.00 25.11 NATOM 67 CA GLU A1012 7.810 7.514 11.602 1.00 24.91 C ATOM 68 CB GLUA1012 8.421 8.737 10.916 1.00 25.40 C ATOM 69 CG GLU A1012 7.413 9.77310.433 1.00 29.98 C ATOM 70 CD GLU A1012 6.857 10.631 11.552 1.00 32.43C ATOM 71 OE1 GLU A1012 5.954 11.447 11.274 1.00 36.73 O ATOM 72 OE2 GLUA1012 7.319 10.497 12.704 1.00 35.01 O ATOM 73 C GLU A1012 6.705 6.95210.716 1.00 24.25 C ATOM 74 O GLU A1012 6.975 6.186 9.789 1.00 22.71 OATOM 75 N GLU A1013 5.462 7.331 11.006 1.00 24.75 N ATOM 76 CA GLU A10134.326 6.895 10.195 1.00 25.26 C ATOM 77 CB GLU A1013 3.006 7.010 10.9561.00 27.28 C ATOM 78 CG GLU A1013 2.782 6.015 12.056 1.00 32.89 C ATOM79 CD GLU A1013 1.337 6.025 12.512 1.00 36.18 C ATOM 80 OE1 GLU A10130.451 5.792 11.661 1.00 38.66 O ATOM 81 OE2 GLU A1013 1.083 6.270 13.7091.00 39.09 O ATOM 82 C GLU A1013 4.253 7.848 9.013 1.00 24.28 C ATOM 83O GLU A1013 4.254 9.062 9.197 1.00 24.07 O ATOM 84 N LEU A1014 4.1797.308 7.805 1.00 23.86 N ATOM 85 CA LEU A1014 4.103 8.149 6.615 1.0024.45 C ATOM 86 CB LEU A1014 4.150 7.274 5.362 1.00 25.54 C ATOM 87 CGLEU A1014 5.402 6.397 5.287 1.00 28.12 C ATOM 88 CD1 LEU A1014 5.2665.386 4.162 1.00 28.37 C ATOM 89 CD2 LEU A1014 6.627 7.284 5.082 1.0029.49 C ATOM 90 C LEU A1014 2.838 9.010 6.611 1.00 23.06 C ATOM 91 O LEUA1014 2.838 10.126 6.083 1.00 22.31 O ATOM 92 N ALA A1015 1.768 8.4907.210 1.00 22.30 N ATOM 93 CA ALA A1015 0.489 9.202 7.284 1.00 21.59 CATOM 94 CB ALA A1015 −0.529 8.372 8.068 1.00 20.65 C ATOM 95 C ALA A10150.664 10.568 7.938 1.00 21.21 C ATOM 96 O ALA A1015 0.101 11.562 7.4831.00 19.58 O ATOM 97 N SER A1016 1.442 10.605 9.017 1.00 21.38 N ATOM 98CA SER A1016 1.711 11.848 9.728 1.00 22.18 C ATOM 99 CB SER A1016 2.58711.569 10.951 1.00 22.67 C ATOM 100 OG SER A1016 2.034 10.523 11.7331.00 29.64 O ATOM 101 C SER A1016 2.428 12.825 8.800 1.00 22.03 C ATOM102 O SER A1016 2.134 14.020 8.786 1.00 24.58 O ATOM 103 N ILE A10173.382 12.319 8.027 1.00 21.56 N ATOM 104 CA ILE A1017 4.112 13.177 7.1041.00 22.10 C ATOM 105 CB ILE A1017 5.336 12.454 6.523 1.00 22.24 C ATOM106 CG2 ILE A1017 5.975 13.312 5.432 1.00 21.89 C ATOM 107 CG1 ILE A10176.342 12.174 7.641 1.00 22.58 C ATOM 108 CD1 ILE A1017 6.904 13.4408.287 1.00 24.27 C ATOM 109 C ILE A1017 3.207 13.633 5.957 1.00 22.93 CATOM 110 O ILE A1017 3.244 14.793 5.549 1.00 23.54 O ATOM 111 N GLUA1018 2.388 12.726 5.440 1.00 23.95 N ATOM 112 CA GLU A1018 1.494 13.0964.348 1.00 26.57 C ATOM 113 CB GLU A1018 0.794 11.862 3.775 1.00 29.38 CATOM 114 CG GLU A1018 −0.244 12.197 2.709 1.00 33.05 C ATOM 115 CD GLUA1018 −0.655 10.987 1.900 1.00 36.21 C ATOM 116 OE1 GLU A1018 −0.8039.897 2.495 1.00 38.49 O ATOM 117 OE2 GLU A1018 −0.840 11.131 0.672 1.0038.02 O ATOM 118 C GLU A1018 0.466 14.116 4.819 1.00 25.75 C ATOM 119 OGLU A1018 0.115 15.032 4.082 1.00 25.64 O ATOM 120 N SER A1019 −0.01113.960 6.052 1.00 27.25 N ATOM 121 CA SER A1019 −0.980 14.893 6.615 1.0027.84 C ATOM 122 CB SER A1019 −1.436 14.425 8.000 1.00 28.92 C ATOM 123OG SER A1019 −2.107 13.176 7.929 1.00 31.15 O ATOM 124 C SER A1019−0.338 16.275 6.734 1.00 28.62 C ATOM 125 O SER A1019 −0.956 17.2896.400 1.00 27.65 O ATOM 126 N ALA A1020 0.907 16.302 7.209 1.00 28.27 NATOM 127 CA ALA A1020 1.650 17.545 7.374 1.00 30.56 C ATOM 128 CB ALAA1020 3.020 17.267 8.005 1.00 30.65 C ATOM 129 C ALA A1020 1.823 18.2676.045 1.00 31.87 C ATOM 130 O ALA A1020 1.686 19.487 5.976 1.00 32.82 OATOM 131 N VAL A1021 2.127 17.513 4.992 1.00 33.76 N ATOM 132 CA VALA1021 2.304 18.099 3.666 1.00 34.05 C ATOM 133 CB VAL A1021 2.830 17.0572.656 1.00 34.30 C ATOM 134 CG1 VAL A1021 2.878 17.660 1.263 1.00 31.58C ATOM 135 CG2 VAL A1021 4.213 16.577 3.073 1.00 33.12 C ATOM 136 C VALA1021 0.969 18.635 3.150 1.00 35.65 C ATOM 137 O VAL A1021 0.891 19.7542.643 1.00 34.17 O ATOM 138 N THR A1022 −0.081 17.829 3.294 1.00 36.17 NATOM 139 CA THR A1022 −1.418 18.209 2.842 1.00 37.29 C ATOM 140 CB THRA1022 −2.433 17.074 3.096 1.00 35.53 C ATOM 141 OG1 THR A1022 −2.10715.955 2.265 1.00 34.37 O ATOM 142 CG2 THR A1022 −3.845 17.530 2.7761.00 35.58 C ATOM 143 C THR A1022 −1.933 19.482 3.504 1.00 39.32 C ATOM144 O THR A1022 −2.672 20.250 2.885 1.00 38.90 O ATOM 145 N ARG A1023−1.544 19.702 4.758 1.00 42.46 N ATOM 146 CA ARG A1023 −1.977 20.8855.496 1.00 46.07 C ATOM 147 CB ARG A1023 −1.684 20.727 6.991 1.00 48.22C ATOM 148 CG ARG A1023 −2.327 19.534 7.664 1.00 51.97 C ATOM 149 CD ARGA1023 −1.900 19.477 9.125 1.00 55.95 C ATOM 150 NE ARG A1023 −2.23418.208 9.770 1.00 59.02 N ATOM 151 CZ ARG A1023 −1.958 17.922 11.0391.00 61.01 C ATOM 152 NH1 ARG A1023 −1.344 18.818 11.804 1.00 61.80 NATOM 153 NH2 ARG A1023 −2.292 16.741 11.546 1.00 61.79 N ATOM 154 C ARGA1023 −1.275 22.147 4.999 1.00 47.81 C ATOM 155 O ARG A1023 −1.80122.888 4.166 1.00 47.51 O ATOM 156 N HIS A1024 −0.077 22.381 5.526 1.0049.48 N ATOM 157 CA HIS A1024 0.714 23.553 5.171 1.00 49.99 C ATOM 158CB HIS A1024 1.238 24.226 6.441 1.00 51.40 C ATOM 159 CG HIS A1024 1.36723.295 7.608 1.00 53.33 C ATOM 160 CD2 HIS A1024 2.447 22.670 8.136 1.0053.80 C ATOM 161 ND1 HIS A1024 0.284 22.885 8.357 1.00 54.21 N ATOM 162CE1 HIS A1024 0.691 22.048 9.295 1.00 54.57 C ATOM 163 NE2 HIS A10241.999 21.900 9.183 1.00 54.28 N ATOM 164 C HIS A1024 1.877 23.218 4.2491.00 49.79 C ATOM 165 O HIS A1024 2.655 22.296 4.513 1.00 49.42 O ATOM166 N GLU A1025 1.987 23.983 3.167 1.00 49.05 N ATOM 167 CA GLU A10253.043 23.796 2.179 1.00 48.04 C ATOM 168 CB GLU A1025 2.813 24.722 0.9841.00 50.62 C ATOM 169 CG GLU A1025 3.876 24.605 −0.092 1.00 54.70 C ATOM170 CD GLU A1025 4.200 25.938 −0.735 1.00 56.22 C ATOM 171 OE1 GLU A10253.295 26.547 −1.343 1.00 58.24 O ATOM 172 OE2 GLU A1025 5.365 26.377−0.627 1.00 58.15 O ATOM 173 C GLU A1025 4.418 24.081 2.768 1.00 45.80 CATOM 174 O GLU A1025 5.433 23.604 2.258 1.00 46.85 O ATOM 175 N GLYA1026 4.447 24.859 3.845 1.00 43.70 N ATOM 176 CA GLY A1026 5.709 25.2024.474 1.00 39.18 C ATOM 177 C GLY A1026 6.425 24.069 5.192 1.00 37.08 CATOM 178 O GLY A1026 7.572 24.235 5.608 1.00 36.56 O ATOM 179 N PHEA1027 5.771 22.920 5.337 1.00 33.78 N ATOM 180 CA PHE A1027 6.390 21.7916.028 1.00 31.60 C ATOM 181 CB PHE A1027 5.397 20.637 6.179 1.00 30.22 CATOM 182 CG PHE A1027 5.951 19.469 6.951 1.00 30.68 C ATOM 183 CD1 PHEA1027 6.224 19.586 8.312 1.00 29.31 C ATOM 184 CD2 PHE A1027 6.23018.266 6.313 1.00 29.88 C ATOM 185 CE1 PHE A1027 6.768 18.523 9.027 1.0031.21 C ATOM 186 CE2 PHE A1027 6.775 17.194 7.020 1.00 30.83 C ATOM 187CZ PHE A1027 7.045 17.326 8.383 1.00 29.69 C ATOM 188 C PHE A1027 7.65321.266 5.345 1.00 29.93 C ATOM 189 O PHE A1027 8.741 21.329 5.908 1.0030.55 O ATOM 190 N ALA A1028 7.504 20.739 4.135 1.00 29.11 N ATOM 191 CAALA A1028 8.637 20.196 3.400 1.00 28.78 C ATOM 192 CB ALA A1028 8.21319.836 1.986 1.00 28.60 C ATOM 193 C ALA A1028 9.779 21.204 3.371 1.0029.38 C ATOM 194 O ALA A1028 10.940 20.850 3.579 1.00 28.07 O ATOM 195 NLYS A1029 9.424 22.463 3.127 1.00 30.57 N ATOM 196 CA LYS A1029 10.37223.574 3.062 1.00 32.15 C ATOM 197 CB LYS A1029 9.608 24.867 2.765 1.0034.73 C ATOM 198 CG LYS A1029 10.076 25.630 1.535 1.00 38.51 C ATOM 199CD LYS A1029 11.365 26.404 1.799 1.00 41.30 C ATOM 200 CE LYS A102911.653 27.390 0.669 1.00 41.77 C ATOM 201 NZ LYS A1029 12.865 28.2140.927 1.00 43.68 N ATOM 202 C LYS A1029 11.173 23.729 4.357 1.00 31.51 CATOM 203 O LYS A1029 12.362 24.043 4.326 1.00 31.47 O ATOM 204 N ARGA1030 10.521 23.512 5.495 1.00 31.52 N ATOM 205 CA ARG A1030 11.19523.626 6.787 1.00 32.17 C ATOM 206 CB ARG A1030 10.188 23.625 7.949 1.0034.49 C ATOM 207 CG ARG A1030 9.287 24.838 8.058 1.00 38.44 C ATOM 208CD ARG A1030 8.775 25.030 9.497 1.00 41.54 C ATOM 209 NE ARG A1030 8.30423.796 10.134 1.00 44.99 N ATOM 210 CZ ARG A1030 9.084 22.932 10.7861.00 47.20 C ATOM 211 NH1 ARG A1030 10.388 23.157 10.898 1.00 48.13 NATOM 212 NH2 ARG A1030 8.562 21.841 11.337 1.00 47.12 N ATOM 213 C ARGA1030 12.145 22.460 7.013 1.00 30.09 C ATOM 214 O ARG A1030 13.24822.631 7.530 1.00 29.93 O ATOM 215 N VAL A1031 11.696 21.272 6.628 1.0027.81 N ATOM 216 CA VAL A1031 12.460 20.050 6.819 1.00 25.50 C ATOM 217CB VAL A1031 11.531 18.806 6.723 1.00 24.73 C ATOM 218 CG1 VAL A103112.355 17.518 6.871 1.00 24.35 C ATOM 219 CG2 VAL A1031 10.465 18.8747.798 1.00 23.33 C ATOM 220 C VAL A1031 13.621 19.835 5.861 1.00 25.01 CATOM 221 O VAL A1031 14.664 19.307 6.252 1.00 25.89 O ATOM 222 N LEUA1032 13.451 20.253 4.617 1.00 24.38 N ATOM 223 CA LEU A1032 14.47220.027 3.604 1.00 25.25 C ATOM 224 CB LEU A1032 13.818 19.409 2.370 1.0025.23 C ATOM 225 CG LEU A1032 12.870 18.230 2.597 1.00 23.47 C ATOM 226CD1 LEU A1032 12.275 17.806 1.266 1.00 23.54 C ATOM 227 CD2 LEU A103213.624 17.072 3.239 1.00 23.54 C ATOM 228 C LEU A1032 15.271 21.2433.169 1.00 25.67 C ATOM 229 O LEU A1032 14.778 22.371 3.184 1.00 25.62 OATOM 230 N THR A1033 16.516 20.997 2.776 1.00 26.32 N ATOM 231 CA THRA1033 17.387 22.057 2.289 1.00 27.40 C ATOM 232 CB THR A1033 18.86221.628 2.283 1.00 27.76 C ATOM 233 OG1 THR A1033 19.015 20.490 1.4251.00 26.35 O ATOM 234 CG2 THR A1033 19.331 21.271 3.691 1.00 28.10 CATOM 235 C THR A1033 16.963 22.275 0.844 1.00 27.65 C ATOM 236 O THRA1033 16.071 21.588 0.350 1.00 27.78 O ATOM 237 N ALA A1034 17.61223.215 0.166 1.00 27.93 N ATOM 238 CA ALA A1034 17.294 23.502 −1.2251.00 28.06 C ATOM 239 CB ALA A1034 18.089 24.717 −1.695 1.00 29.35 CATOM 240 C ALA A1034 17.594 22.296 −2.119 1.00 27.67 C ATOM 241 O ALAA1034 16.791 21.940 −2.981 1.00 28.26 O ATOM 242 N LEU A1035 18.75221.675 −1.918 1.00 27.21 N ATOM 243 CA LEU A1035 19.131 20.510 −2.7111.00 29.21 C ATOM 244 CB LEU A1035 20.531 20.015 −2.318 1.00 28.90 CATOM 245 CG LEU A1035 21.743 20.903 −2.634 1.00 32.48 C ATOM 246 CD1 LEUA1035 22.960 20.382 −1.877 1.00 31.19 C ATOM 247 CD2 LEU A1035 22.01720.924 −4.137 1.00 32.53 C ATOM 248 C LEU A1035 18.111 19.388 −2.5141.00 27.97 C ATOM 249 O LEU A1035 17.674 18.758 −3.475 1.00 28.70 O ATOM250 N GLU A1036 17.731 19.143 −1.267 1.00 27.27 N ATOM 251 CA GLU A103616.757 18.100 −0.980 1.00 27.49 C ATOM 252 CB GLU A1036 16.599 17.9380.532 1.00 27.41 C ATOM 253 CG GLU A1036 17.760 17.195 1.186 1.00 24.80C ATOM 254 CD GLU A1036 17.720 17.252 2.703 1.00 26.22 C ATOM 255 OE1GLU A1036 18.225 16.306 3.345 1.00 25.82 O ATOM 256 OE2 GLU A1036 17.20118.248 3.256 1.00 26.57 O ATOM 257 C GLU A1036 15.413 18.416 −1.634 1.0027.55 C ATOM 258 O GLU A1036 14.740 17.522 −2.138 1.00 25.83 O ATOM 259N MET A1037 15.031 19.691 −1.640 1.00 28.35 N ATOM 260 CA MET A103713.765 20.099 −2.247 1.00 29.92 C ATOM 261 CB MET A1037 13.529 21.599−2.069 1.00 30.37 C ATOM 262 CG MET A1037 12.985 22.000 −0.714 1.0033.04 C ATOM 263 SD MET A1037 11.412 21.198 −0.336 1.00 35.56 S ATOM 264CE MET A1037 10.356 21.852 −1.624 1.00 33.04 C ATOM 265 C MET A103713.758 19.779 −3.731 1.00 31.19 C ATOM 266 O MET A1037 12.711 19.461−4.306 1.00 30.89 O ATOM 267 N GLU A1038 14.928 19.881 −4.352 1.00 31.50N ATOM 268 CA GLU A1038 15.049 19.600 −5.774 1.00 33.14 C ATOM 269 CBGLU A1038 16.499 19.777 −6.233 1.00 34.77 C ATOM 270 CG GLU A1038 17.00521.208 −6.093 1.00 39.68 C ATOM 271 CD GLU A1038 18.411 21.400 −6.6391.00 41.20 C ATOM 272 OE1 GLU A1038 18.981 22.492 −6.434 1.00 44.15 OATOM 273 OE2 GLU A1038 18.943 20.467 −7.276 1.00 42.51 O ATOM 274 C GLUA1038 14.570 18.186 −6.066 1.00 31.14 C ATOM 275 O GLU A1038 13.77317.974 −6.976 1.00 31.21 O ATOM 276 N ARG A1039 15.039 17.215 −5.2901.00 29.70 N ATOM 277 CA ARG A1039 14.606 15.844 −5.521 1.00 28.01 CATOM 278 CB ARG A1039 15.499 14.846 −4.778 1.00 29.96 C ATOM 279 CG ARGA1039 15.061 13.406 −5.005 1.00 30.43 C ATOM 280 CD ARG A1039 16.21312.420 −4.969 1.00 30.42 C ATOM 281 NE ARG A1039 15.723 11.046 −5.0851.00 31.83 N ATOM 282 CZ ARG A1039 15.203 10.509 −6.188 1.00 32.36 CATOM 283 NH1 ARG A1039 15.098 11.214 −7.310 1.00 30.37 N ATOM 284 NH2ARG A1039 14.764 9.258 −6.161 1.00 32.43 N ATOM 285 C ARG A1039 13.15815.671 −5.086 1.00 26.14 C ATOM 286 O ARG A1039 12.367 15.046 −5.7851.00 25.25 O ATOM 287 N PHE A1040 12.808 16.233 −3.934 1.00 24.86 N ATOM288 CA PHE A1040 11.441 16.132 −3.430 1.00 26.03 C ATOM 289 CB PHE A104011.273 17.007 −2.178 1.00 25.44 C ATOM 290 CG PHE A1040 9.861 17.056−1.657 1.00 26.41 C ATOM 291 CD1 PHE A1040 9.298 15.953 −1.027 1.0025.83 C ATOM 292 CD2 PHE A1040 9.080 18.194 −1.838 1.00 26.12 C ATOM 293CE1 PHE A1040 7.977 15.977 −0.585 1.00 24.52 C ATOM 294 CE2 PHE A10407.752 18.232 −1.399 1.00 26.23 C ATOM 295 CZ PHE A1040 7.202 17.119−0.772 1.00 23.77 C ATOM 296 C PHE A1040 10.412 16.548 −4.488 1.00 26.70C ATOM 297 O PHE A1040 9.438 15.837 −4.731 1.00 29.10 O ATOM 298 N THRA1041 10.635 17.691 −5.126 1.00 28.25 N ATOM 299 CA THR A1041 9.70518.195 −6.136 1.00 30.17 C ATOM 300 CB THR A1041 9.935 19.700 −6.3911.00 31.11 C ATOM 301 OG1 THR A1041 11.255 19.911 −6.904 1.00 32.37 OATOM 302 CG2 THR A1041 9.781 20.478 −5.099 1.00 29.66 C ATOM 303 C THRA1041 9.751 17.456 −7.474 1.00 31.98 C ATOM 304 O THR A1041 8.863 17.627−8.311 1.00 32.84 O ATOM 305 N SER A1042 10.781 16.637 −7.673 1.00 31.91N ATOM 306 CA SER A1042 10.933 15.869 −8.909 1.00 32.77 C ATOM 307 CBSER A1042 12.416 15.609 −9.192 1.00 33.18 C ATOM 308 OG SER A1042 13.10616.820 −9.448 1.00 38.29 O ATOM 309 C SER A1042 10.215 14.529 −8.8311.00 32.24 C ATOM 310 O SER A1042 10.071 13.834 −9.840 1.00 32.01 O ATOM311 N LEU A1043 9.766 14.175 −7.630 1.00 29.92 N ATOM 312 CA LEU A10439.101 12.901 −7.394 1.00 28.48 C ATOM 313 CB LEU A1043 9.541 12.332−6.043 1.00 23.86 C ATOM 314 CG LEU A1043 11.050 12.097 −5.928 1.0022.34 C ATOM 315 CD1 LEU A1043 11.391 11.610 −4.538 1.00 16.25 C ATOM316 CD2 LEU A1043 11.493 11.073 −6.977 1.00 20.12 C ATOM 317 C LEU A10437.587 12.967 −7.454 1.00 30.04 C ATOM 318 O LEU A1043 6.995 14.045−7.415 1.00 29.66 O ATOM 319 N LYS A1044 6.970 11.793 −7.524 1.00 30.79N ATOM 320 CA LYS A1044 5.525 11.679 −7.633 1.00 32.89 C ATOM 321 CB LYSA1044 5.167 11.102 −9.008 1.00 36.71 C ATOM 322 CG LYS A1044 5.59811.946 −10.199 1.00 40.80 C ATOM 323 CD LYS A1044 4.583 13.041 −10.5001.00 45.23 C ATOM 324 CE LYS A1044 4.793 13.615 −11.897 1.00 47.01 CATOM 325 NZ LYS A1044 3.591 14.354 −12.387 1.00 48.79 N ATOM 326 C LYSA1044 4.883 10.801 −6.564 1.00 31.67 C ATOM 327 O LYS A1044 5.512 9.894−6.017 1.00 31.18 O ATOM 328 N GLY A1045 3.611 11.080 −6.299 1.00 30.41N ATOM 329 CA GLY A1045 2.834 10.321 −5.337 1.00 31.09 C ATOM 330 C GLYA1045 3.518 9.841 −4.074 1.00 31.50 C ATOM 331 O GLY A1045 4.098 10.631−3.329 1.00 32.31 O ATOM 332 N ARG A1046 3.435 8.534 −3.841 1.00 31.79 NATOM 333 CA ARG A1046 4.009 7.904 −2.659 1.00 34.20 C ATOM 334 CB ARGA1046 3.791 6.386 −2.717 1.00 37.24 C ATOM 335 CG ARG A1046 2.420 5.971−3.239 1.00 43.96 C ATOM 336 CD ARG A1046 2.301 4.457 −3.386 1.00 48.00C ATOM 337 NE ARG A1046 1.885 3.810 −2.144 1.00 52.29 N ATOM 338 CZ ARGA1046 1.793 2.493 −1.980 1.00 53.80 C ATOM 339 NH1 ARG A1046 1.399 1.995−0.815 1.00 54.77 N ATOM 340 NH2 ARG A1046 2.106 1.673 −2.975 1.00 56.31N ATOM 341 C ARG A1046 5.499 8.194 −2.516 1.00 32.21 C ATOM 342 O ARGA1046 5.972 8.529 −1.433 1.00 32.82 O ATOM 343 N ARG A1047 6.234 8.060−3.614 1.00 31.05 N ATOM 344 CA ARG A1047 7.670 8.292 −3.605 1.00 30.41C ATOM 345 CB ARG A1047 8.235 8.126 −5.015 1.00 32.83 C ATOM 346 CG ARGA1047 9.252 7.013 −5.123 1.00 37.44 C ATOM 347 CD ARG A1047 8.909 6.055−6.246 1.00 40.57 C ATOM 348 NE ARG A1047 9.734 4.854 −6.183 1.00 45.77N ATOM 349 CZ ARG A1047 9.635 3.835 −7.028 1.00 47.39 C ATOM 350 NH1 ARGA1047 10.428 2.780 −6.896 1.00 49.29 N ATOM 351 NH2 ARG A1047 8.7433.873 −8.008 1.00 48.96 N ATOM 352 C ARG A1047 8.040 9.668 −3.062 1.0028.90 C ATOM 353 O ARG A1047 9.006 9.808 −2.307 1.00 27.20 O ATOM 354 NGLN A1048 7.268 10.680 −3.444 1.00 26.75 N ATOM 355 CA GLN A1048 7.52212.042 −2.993 1.00 25.72 C ATOM 356 CB GLN A1048 6.552 13.014 −3.6791.00 26.20 C ATOM 357 CG GLN A1048 6.972 14.472 −3.555 1.00 26.13 C ATOM358 CD GLN A1048 6.169 15.400 −4.449 1.00 25.31 C ATOM 359 OE1 GLN A10486.618 16.495 −4.773 1.00 27.04 O ATOM 360 NE2 GLN A1048 4.977 14.970−4.843 1.00 24.57 N ATOM 361 C GLN A1048 7.390 12.162 −1.475 1.00 23.82C ATOM 362 O GLN A1048 8.225 12.783 −0.819 1.00 23.93 O ATOM 363 N ILEA1049 6.340 11.568 −0.919 1.00 23.76 N ATOM 364 CA ILE A1049 6.12611.615 0.523 1.00 23.77 C ATOM 365 CB ILE A1049 4.733 11.084 0.900 1.0025.38 C ATOM 366 CG2 ILE A1049 4.598 11.001 2.401 1.00 25.87 C ATOM 367CG1 ILE A1049 3.657 11.999 0.315 1.00 26.78 C ATOM 368 CD1 ILE A10493.787 13.453 0.751 1.00 30.33 C ATOM 369 C ILE A1049 7.181 10.776 1.2281.00 22.10 C ATOM 370 O ILE A1049 7.673 11.150 2.283 1.00 21.61 O ATOM371 N GLU A1050 7.525 9.642 0.631 1.00 22.60 N ATOM 372 CA GLU A10508.532 8.755 1.200 1.00 23.30 C ATOM 373 CB GLU A1050 8.667 7.478 0.3631.00 23.16 C ATOM 374 CG GLU A1050 9.889 6.659 0.739 1.00 28.58 C ATOM375 CD GLU A1050 9.978 6.445 2.234 1.00 29.28 C ATOM 376 OE1 GLU A105011.108 6.330 2.760 1.00 30.35 O ATOM 377 OE2 GLU A1050 8.909 6.394 2.8821.00 30.91 O ATOM 378 C GLU A1050 9.885 9.454 1.279 1.00 22.26 C ATOM379 O GLU A1050 10.627 9.288 2.253 1.00 23.12 O ATOM 380 N TYR A105110.209 10.245 0.262 1.00 22.07 N ATOM 381 CA TYR A1051 11.478 10.9480.262 1.00 21.63 C ATOM 382 CB TYR A1051 11.686 11.704 −1.054 1.00 20.34C ATOM 383 CG TYR A1051 12.992 12.472 −1.082 1.00 20.50 C ATOM 384 CD1TYR A1051 13.055 13.801 −0.659 1.00 20.43 C ATOM 385 CE1 TYR A105114.269 14.490 −0.621 1.00 20.01 C ATOM 386 CD2 TYR A1051 14.179 11.849−1.475 1.00 20.86 C ATOM 387 CE2 TYR A1051 15.400 12.531 −1.441 1.0021.25 C ATOM 388 CZ TYR A1051 15.432 13.852 −1.010 1.00 19.89 C ATOM 389OH TYR A1051 16.630 14.525 −0.959 1.00 20.04 O ATOM 390 C TYR A105111.557 11.920 1.434 1.00 21.88 C ATOM 391 O TYR A1051 12.557 11.9632.152 1.00 20.59 O ATOM 392 N LEU A1052 10.499 12.702 1.621 1.00 21.63 NATOM 393 CA LEU A1052 10.452 13.671 2.706 1.00 21.68 C ATOM 394 CB LEUA1052 9.179 14.513 2.590 1.00 20.47 C ATOM 395 CG LEU A1052 8.808 15.4183.765 1.00 22.03 C ATOM 396 CD1 LEU A1052 9.962 16.348 4.120 1.00 21.80C ATOM 397 CD2 LEU A1052 7.566 16.209 3.381 1.00 20.67 C ATOM 398 C LEUA1052 10.504 12.964 4.055 1.00 20.98 C ATOM 399 O LEU A1052 11.31413.306 4.919 1.00 21.63 O ATOM 400 N ALA A1053 9.639 11.971 4.223 1.0019.65 N ATOM 401 CA ALA A1053 9.578 11.190 5.457 1.00 18.20 C ATOM 402CB ALA A1053 8.567 10.054 5.299 1.00 18.13 C ATOM 403 C ALA A1053 10.95210.614 5.818 1.00 17.32 C ATOM 404 O ALA A1053 11.356 10.642 6.982 1.0015.65 O ATOM 405 N GLY A1054 11.660 10.092 4.816 1.00 16.84 N ATOM 406CA GLY A1054 12.978 9.516 5.049 1.00 16.81 C ATOM 407 C GLY A1054 13.98110.540 5.542 1.00 16.80 C ATOM 408 O GLY A1054 14.788 10.270 6.439 1.0016.69 O ATOM 409 N ARG A1055 13.946 11.728 4.952 1.00 18.02 N ATOM 410CA ARG A1055 14.866 12.772 5.364 1.00 18.20 C ATOM 411 CB ARG A105514.811 13.928 4.371 1.00 19.98 C ATOM 412 CG ARG A1055 15.908 13.8733.303 1.00 19.89 C ATOM 413 CD ARG A1055 15.963 12.534 2.565 1.00 21.10C ATOM 414 NE ARG A1055 17.109 12.487 1.652 1.00 21.61 N ATOM 415 CZ ARGA1055 17.449 11.426 0.925 1.00 21.69 C ATOM 416 NH1 ARG A1055 16.73010.311 0.999 1.00 20.97 N ATOM 417 NH2 ARG A1055 18.508 11.481 0.1221.00 17.88 N ATOM 418 C ARG A1055 14.534 13.243 6.781 1.00 18.74 C ATOM419 O ARG A1055 15.433 13.506 7.585 1.00 16.13 O ATOM 420 N TRP A105613.243 13.324 7.086 1.00 17.18 N ATOM 421 CA TRP A1056 12.793 13.7328.412 1.00 19.43 C ATOM 422 CB TRP A1056 11.267 13.703 8.468 1.00 21.99C ATOM 423 CG TRP A1056 10.694 14.264 9.713 1.00 26.53 C ATOM 424 CD2TRP A1056 10.311 13.533 10.877 1.00 28.20 C ATOM 425 CE2 TRP A1056 9.81614.468 11.813 1.00 28.53 C ATOM 426 CE3 TRP A1056 10.333 12.177 11.2221.00 29.04 C ATOM 427 CD1 TRP A1056 10.431 15.581 9.978 1.00 26.38 CATOM 428 NE1 TRP A1056 9.905 15.708 11.237 1.00 29.97 N ATOM 429 CZ2 TRPA1056 9.347 14.090 13.073 1.00 30.15 C ATOM 430 CZ3 TRP A1056 9.86811.801 12.476 1.00 31.30 C ATOM 431 CH2 TRP A1056 9.379 12.755 13.3861.00 31.45 C ATOM 432 C TRP A1056 13.343 12.710 9.412 1.00 18.72 C ATOM433 O TRP A1056 13.992 13.063 10.397 1.00 16.51 O ATOM 434 N SER A105713.084 11.435 9.137 1.00 17.50 N ATOM 435 CA SER A1057 13.532 10.35210.011 1.00 19.23 C ATOM 436 CB SER A1057 13.053 9.009 9.448 1.00 21.41C ATOM 437 OG SER A1057 13.243 7.971 10.388 1.00 25.06 O ATOM 438 C SERA1057 15.053 10.320 10.201 1.00 19.01 C ATOM 439 O SER A1057 15.54910.120 11.317 1.00 19.71 O ATOM 440 N ALA A1058 15.789 10.511 9.111 1.0016.54 N ATOM 441 CA ALA A1058 17.243 10.495 9.162 1.00 16.02 C ATOM 442CB ALA A1058 17.798 10.607 7.757 1.00 15.16 C ATOM 443 C ALA A105817.790 11.616 10.035 1.00 15.70 C ATOM 444 O ALA A1058 18.707 11.41110.836 1.00 16.78 O ATOM 445 N LYS A1059 17.221 12.805 9.884 1.00 16.69N ATOM 446 CA LYS A1059 17.664 13.957 10.648 1.00 18.17 C ATOM 447 CBLYS A1059 17.079 15.240 10.042 1.00 18.92 C ATOM 448 CG LYS A1059 17.53615.450 8.588 1.00 19.75 C ATOM 449 CD LYS A1059 17.059 16.773 8.003 1.0019.99 C ATOM 450 CE LYS A1059 17.531 16.933 6.549 1.00 19.86 C ATOM 451NZ LYS A1059 17.304 18.322 6.031 1.00 20.25 N ATOM 452 C LYS A105917.302 13.818 12.116 1.00 19.11 C ATOM 453 O LYS A1059 18.067 14.22212.995 1.00 18.56 O ATOM 454 N GLU A1060 16.143 13.225 12.374 1.00 18.52N ATOM 455 CA GLU A1060 15.679 12.998 13.736 1.00 21.84 C ATOM 456 CBGLU A1060 14.247 12.448 13.704 1.00 26.26 C ATOM 457 CG GLU A1060 13.42812.722 14.952 1.00 33.87 C ATOM 458 CD GLU A1060 13.083 14.192 15.1301.00 35.47 C ATOM 459 OE1 GLU A1060 12.298 14.733 14.322 1.00 38.74 OATOM 460 OE2 GLU A1060 13.601 14.811 16.082 1.00 39.14 O ATOM 461 O GLUA1060 16.631 11.982 14.390 1.00 21.03 C ATOM 462 O GLU A1060 17.04512.149 15.544 1.00 18.91 O ATOM 463 N ALA A1061 16.991 10.943 13.6351.00 18.55 N ATOM 464 CA ALA A1061 17.898 9.910 14.131 1.00 18.39 C ATOM465 CB ALA A1061 18.017 8.777 13.113 1.00 15.08 C ATOM 466 C ALA A106119.283 10.490 14.429 1.00 18.00 C ATOM 467 O ALA A1061 19.905 10.15115.436 1.00 17.16 O ATOM 468 N PHE A1062 19.768 11.352 13.542 1.00 18.20N ATOM 469 CA PHE A1062 21.069 11.970 13.741 1.00 20.25 C ATOM 470 CBPHE A1062 21.433 12.855 12.546 1.00 20.89 C ATOM 471 CG PHE A1062 22.72113.605 12.730 1.00 23.32 C ATOM 472 CD1 PHE A1062 22.761 14.776 13.4891.00 24.72 C ATOM 473 CD2 PHE A1062 23.908 13.112 12.194 1.00 23.55 CATOM 474 CE1 PHE A1062 23.973 15.443 13.717 1.00 24.71 C ATOM 475 CE2PHE A1062 25.119 13.766 12.414 1.00 23.92 C ATOM 476 CZ PHE A1062 25.15014.934 13.179 1.00 25.42 C ATOM 477 C PHE A1062 21.090 12.800 15.0261.00 21.33 C ATOM 478 O PHE A1062 22.035 12.726 15.809 1.00 20.18 O ATOM479 N SER A1063 20.045 13.593 15.244 1.00 22.52 N ATOM 480 CA SER A106319.973 14.420 16.445 1.00 24.40 C ATOM 481 CB SER A1063 18.679 15.23016.447 1.00 25.96 C ATOM 482 OG SER A1063 18.670 16.112 15.338 1.0030.50 O ATOM 483 C SER A1063 20.060 13.562 17.704 1.00 24.30 C ATOM 484O SER A1063 20.714 13.938 18.682 1.00 23.77 O ATOM 485 N LYS A106419.407 12.406 17.678 1.00 22.33 N ATOM 486 CA LYS A1064 19.451 11.51318.823 1.00 23.04 C ATOM 487 CB LYS A1064 18.405 10.406 18.684 1.0023.38 C ATOM 488 CG LYS A1064 16.971 10.881 18.903 1.00 25.10 C ATOM 489CD LYS A1064 15.986 9.734 18.726 1.00 28.41 C ATOM 490 CE LYS A106414.548 10.194 18.924 1.00 32.98 C ATOM 491 NZ LYS A1064 13.566 9.19518.410 1.00 35.52 N ATOM 492 C LYS A1064 20.845 10.907 18.949 1.00 22.52C ATOM 493 O LYS A1064 21.285 10.572 20.047 1.00 21.41 O ATOM 494 N ALAA1065 21.539 10.774 17.820 1.00 21.47 N ATOM 495 CA ALA A1065 22.88510.220 17.826 1.00 22.53 C ATOM 496 CB ALA A1065 23.379 9.980 16.3991.00 20.33 C ATOM 497 C ALA A1065 23.796 11.207 18.537 1.00 24.41 C ATOM498 O ALA A1065 24.751 10.811 19.201 1.00 24.00 O ATOM 499 N MET A106623.499 12.496 18.390 1.00 28.05 N ATOM 500 CA MET A1066 24.283 13.53019.049 1.00 32.04 C ATOM 501 CB MET A1066 24.167 14.859 18.309 1.0034.23 C ATOM 502 CG MET A1066 24.913 14.895 16.997 1.00 40.28 C ATOM 503SD MET A1066 25.423 16.574 16.602 1.00 48.25 S ATOM 504 CE MET A106627.174 16.492 17.024 1.00 46.99 C ATOM 505 C MET A1066 23.826 13.71620.493 1.00 33.24 C ATOM 506 O MET A1066 24.456 14.443 21.254 1.00 33.60O ATOM 507 N GLY A1067 22.720 13.069 20.856 1.00 33.56 N ATOM 508 CA GLYA1067 22.217 13.159 22.216 1.00 34.99 C ATOM 509 C GLY A1067 21.31114.339 22.519 1.00 36.72 C ATOM 510 O GLY A1067 21.237 14.787 23.6661.00 34.92 O ATOM 511 N THR A1068 20.616 14.845 21.504 1.00 38.07 N ATOM512 CA THR A1068 19.716 15.975 21.699 1.00 39.81 C ATOM 513 CB THR A106820.455 17.316 21.504 1.00 40.69 C ATOM 514 OG1 THR A1068 19.535 18.40021.687 1.00 42.07 O ATOM 515 CG2 THR A1068 21.062 17.396 20.114 1.0040.32 C ATOM 516 C THR A1068 18.520 15.922 20.752 1.00 40.62 C ATOM 517O THR A1068 18.293 14.915 20.077 1.00 41.29 O ATOM 518 N GLY A106917.753 17.007 20.716 1.00 40.61 N ATOM 519 CA GLY A1069 16.586 17.06119.856 1.00 40.92 C ATOM 520 C GLY A1069 16.835 17.849 18.587 1.00 40.96C ATOM 521 O GLY A1069 17.705 18.722 18.547 1.00 41.30 O ATOM 522 N ILEA1070 16.065 17.545 17.547 1.00 40.13 N ATOM 523 CA ILE A1070 16.20718.224 16.266 1.00 40.90 C ATOM 524 CB ILE A1070 15.288 17.591 15.2001.00 40.70 C ATOM 525 CG2 ILE A1070 13.828 17.774 15.593 1.00 40.55 CATOM 526 CG1 ILE A1070 15.557 18.227 13.835 1.00 41.43 C ATOM 527 CD1ILE A1070 16.980 18.055 13.352 1.00 39.85 C ATOM 528 C ILE A1070 15.87619.712 16.387 1.00 41.49 C ATOM 529 O ILE A1070 16.354 20.533 15.5981.00 41.31 O ATOM 530 N SER A1071 15.058 20.054 17.379 1.00 41.78 N ATOM531 CA SER A1071 14.672 21.442 17.594 1.00 42.83 C ATOM 532 CB SER A107113.546 21.531 18.633 1.00 43.42 C ATOM 533 OG SER A1071 13.938 20.98019.877 1.00 44.55 O ATOM 534 C SER A1071 15.856 22.295 18.039 1.00 43.32C ATOM 535 O SER A1071 15.792 23.523 17.984 1.00 44.46 O ATOM 536 N LYSA1072 16.938 21.648 18.472 1.00 42.56 N ATOM 537 CA LYS A1072 18.12322.377 18.911 1.00 41.56 C ATOM 538 CB LYS A1072 18.744 21.706 20.1411.00 41.25 C ATOM 539 CG LYS A1072 19.600 20.489 19.844 0.05 41.20 CATOM 540 CD LYS A1072 21.069 20.860 19.724 0.05 41.09 C ATOM 541 CE LYSA1072 21.602 21.414 21.037 0.05 41.02 C ATOM 542 NZ LYS A1072 21.47020.437 22.152 0.05 40.94 N ATOM 543 C LYS A1072 19.139 22.462 17.7771.00 41.40 C ATOM 544 O LYS A1072 19.840 23.462 17.643 1.00 41.76 O ATOM545 N LEU A1073 19.220 21.413 16.960 1.00 40.37 N ATOM 546 CA LEU A107320.142 21.411 15.829 1.00 38.42 C ATOM 547 CB LEU A1073 20.439 19.98515.339 1.00 39.84 C ATOM 548 CG LEU A1073 21.489 19.100 16.015 1.0040.56 C ATOM 549 CD1 LEU A1073 22.585 19.956 16.635 1.00 41.19 C ATOM550 CD2 LEU A1073 20.820 18.243 17.064 1.00 42.23 C ATOM 551 C LEU A107319.556 22.198 14.664 1.00 36.59 C ATOM 552 O LEU A1073 20.205 23.09114.123 1.00 36.83 O ATOM 553 N GLY A1074 18.326 21.849 14.285 1.00 34.67N ATOM 554 CA GLY A1074 17.653 22.500 13.172 1.00 31.12 C ATOM 555 C GLYA1074 17.746 21.631 11.927 1.00 29.81 C ATOM 556 O GLY A1074 18.83021.176 11.576 1.00 29.20 O ATOM 557 N PHE A1075 16.619 21.396 11.2601.00 29.29 N ATOM 558 CA PHE A1075 16.595 20.565 10.051 1.00 29.15 CATOM 559 CB PHE A1075 15.163 20.442 9.502 1.00 28.80 C ATOM 560 CG PHEA1075 14.244 19.610 10.353 1.00 29.16 C ATOM 561 CD1 PHE A1075 13.30620.212 11.183 1.00 29.51 C ATOM 562 CD2 PHE A1075 14.309 18.221 10.3151.00 28.39 C ATOM 563 CE1 PHE A1075 12.440 19.443 11.964 1.00 28.84 CATOM 564 CE2 PHE A1075 13.451 17.445 11.089 1.00 30.94 C ATOM 565 CZ PHEA1075 12.514 18.059 11.916 1.00 29.27 C ATOM 566 C PHE A1075 17.50021.072 8.922 1.00 29.25 C ATOM 567 O PHE A1075 18.096 20.275 8.193 1.0027.78 O ATOM 568 N GLN A1076 17.589 22.393 8.772 1.00 29.64 N ATOM 569CA GLN A1076 18.397 23.008 7.717 1.00 29.73 C ATOM 570 CB GLN A107618.046 24.497 7.593 1.00 31.55 C ATOM 571 CG GLN A1076 16.585 24.7467.253 1.00 31.77 C ATOM 572 CD GLN A1076 16.202 24.181 5.895 1.00 32.15C ATOM 573 OE1 GLN A1076 15.044 23.849 5.652 1.00 34.09 O ATOM 574 NE2GLN A1076 17.174 24.084 5.002 1.00 32.35 N ATOM 575 C GLN A1076 19.88822.845 7.975 1.00 31.01 C ATOM 576 O GLN A1076 20.724 23.105 7.099 1.0030.59 O ATOM 577 N ASP A1077 20.211 22.401 9.183 1.00 30.30 N ATOM 578CA ASP A1077 21.592 22.182 9.588 1.00 30.99 C ATOM 579 CB ASP A107721.684 22.266 11.111 1.00 34.42 C ATOM 580 CG ASP A1077 22.894 23.03411.578 1.00 38.94 C ATOM 581 OD1 ASP A1077 24.025 22.549 11.358 1.0040.63 O ATOM 582 OD2 ASP A1077 22.710 24.127 12.162 1.00 41.18 O ATOM583 C ASP A1077 22.066 20.803 9.114 1.00 28.98 C ATOM 584 O ASP A107723.247 20.470 9.198 1.00 27.03 O ATOM 585 N LEU A1078 21.134 19.9988.622 1.00 26.47 N ATOM 586 CA LEU A1078 21.472 18.665 8.155 1.00 25.11C ATOM 587 CB LEU A1078 20.782 17.614 9.029 1.00 25.83 C ATOM 588 CG LEUA1078 21.066 17.667 10.529 1.00 25.61 C ATOM 589 CD1 LEU A1078 20.07516.787 11.291 1.00 26.16 C ATOM 590 CD2 LEU A1078 22.494 17.227 10.7751.00 26.52 C ATOM 591 C LEU A1078 21.015 18.495 6.723 1.00 24.62 C ATOM592 O LEU A1078 20.052 19.125 6.296 1.00 25.13 O ATOM 593 N GLU A107921.710 17.648 5.975 1.00 23.38 N ATOM 594 CA GLU A1079 21.312 17.3884.603 1.00 22.76 C ATOM 595 CB GLU A1079 22.008 18.338 3.639 1.00 24.57C ATOM 596 CG GLU A1079 21.425 18.299 2.241 1.00 25.55 C ATOM 597 CD GLUA1079 22.219 19.146 1.274 1.00 28.95 C ATOM 598 OE1 GLU A1079 23.41518.844 1.074 1.00 28.46 O ATOM 599 OE2 GLU A1079 21.652 20.114 0.7221.00 31.06 O ATOM 600 C GLU A1079 21.639 15.958 4.220 1.00 21.67 C ATOM601 O GLU A1079 22.747 15.476 4.458 1.00 21.79 O ATOM 602 N VAL A108020.667 15.283 3.626 1.00 18.92 N ATOM 603 CA VAL A1080 20.861 13.9043.208 1.00 19.27 C ATOM 604 CB VAL A1080 19.836 12.967 3.881 1.00 18.84C ATOM 605 CG1 VAL A1080 20.181 11.504 3.578 1.00 18.64 C ATOM 606 CG2VAL A1080 19.801 13.230 5.368 1.00 18.66 C ATOM 607 C VAL A1080 20.69013.798 1.696 1.00 19.85 C ATOM 608 O VAL A1080 19.596 14.003 1.169 1.0019.06 O ATOM 609 N LEU A1081 21.780 13.497 1.003 1.00 19.76 N ATOM 610CA LEU A1081 21.742 13.332 −0.442 1.00 20.15 C ATOM 611 CB LEU A108122.808 14.210 −1.111 1.00 19.63 C ATOM 612 CG LEU A1081 22.640 15.717−0.878 1.00 19.82 C ATOM 613 CD1 LEU A1081 23.817 16.488 −1.475 1.0019.43 C ATOM 614 CD2 LEU A1081 21.326 16.171 −1.485 1.00 18.80 C ATOM615 C LEU A1081 22.037 11.861 −0.696 1.00 20.78 C ATOM 616 O LEU A108122.097 11.067 0.242 1.00 19.52 O ATOM 617 N ASN A1082 22.224 11.495−1.957 1.00 21.64 N ATOM 618 CA ASN A1082 22.521 10.110 −2.301 1.0022.51 C ATOM 619 CB ASN A1082 21.430 9.574 −3.230 1.00 21.83 C ATOM 620CG ASN A1082 20.134 9.281 −2.485 1.00 24.97 C ATOM 621 OD1 ASN A108219.930 8.174 −1.973 1.00 26.72 O ATOM 622 ND2 ASN A1082 19.264 10.275−2.402 1.00 23.64 N ATOM 623 C ASN A1082 23.897 10.029 −2.954 1.00 22.59C ATOM 624 O ASN A1082 24.196 10.786 −3.876 1.00 23.10 O ATOM 625 N ASNA1083 24.738 9.118 −2.472 1.00 21.81 N ATOM 626 CA ASN A1083 26.0798.998 −3.021 1.00 24.05 C ATOM 627 CB ASN A1083 27.011 8.298 −2.018 1.0021.32 C ATOM 628 CG ASN A1083 26.634 6.849 −1.748 1.00 23.86 C ATOM 629OD1 ASN A1083 27.083 6.269 −0.752 1.00 23.67 O ATOM 630 ND2 ASN A108325.835 6.249 −2.631 1.00 20.56 N ATOM 631 C ASN A1083 26.112 8.315−4.385 1.00 26.50 C ATOM 632 O ASN A1083 25.065 7.986 −4.951 1.00 25.00O ATOM 633 N GLU A1084 27.313 8.118 −4.921 1.00 28.34 N ATOM 634 CA GLUA1084 27.447 7.514 −6.237 1.00 32.10 C ATOM 635 CB GLU A1084 28.9077.561 −6.700 1.00 32.77 C ATOM 636 CG GLU A1084 29.885 6.749 −5.877 1.0035.30 C ATOM 637 CD GLU A1084 31.327 7.041 −6.263 1.00 38.54 C ATOM 638OE1 GLU A1084 31.628 7.058 −7.478 1.00 39.35 O ATOM 639 OE2 GLU A108432.160 7.252 −5.356 1.00 40.56 O ATOM 640 C GLU A1084 26.906 6.092−6.307 1.00 32.37 C ATOM 641 O GLU A1084 26.582 5.610 −7.386 1.00 34.17O ATOM 642 N ARG A1085 26.811 5.426 −5.158 1.00 31.86 N ATOM 643 CA ARGA1085 26.278 4.069 −5.111 1.00 29.86 C ATOM 644 CB ARG A1085 26.9673.259 −4.009 1.00 30.40 C ATOM 645 CG ARG A1085 28.442 2.992 −4.269 0.0530.17 C ATOM 646 CD ARG A1085 28.668 2.173 −5.540 0.05 30.07 C ATOM 647NE ARG A1085 28.539 0.730 −5.333 0.05 30.12 N ATOM 648 CZ ARG A108527.396 0.089 −5.107 0.05 30.07 C ATOM 649 NH1 ARG A1085 26.249 0.751−5.054 0.05 30.16 N ATOM 650 NH2 ARG A1085 27.401 −1.226 −4.938 0.0530.04 N ATOM 651 C ARG A1085 24.768 4.117 −4.860 1.00 28.84 C ATOM 652 OARG A1085 24.121 3.084 −4.683 1.00 28.73 O ATOM 653 N GLY A1086 24.2225.329 −4.842 1.00 26.09 N ATOM 654 CA GLY A1086 22.797 5.514 −4.635 1.0024.49 C ATOM 655 C GLY A1086 22.286 5.493 −3.202 1.00 23.98 C ATOM 656 OGLY A1086 21.090 5.649 −2.975 1.00 25.43 O ATOM 657 N ALA A1087 23.1725.306 −2.233 1.00 21.90 N ATOM 658 CA ALA A1087 22.755 5.259 −0.836 1.0021.27 C ATOM 659 CB ALA A1087 23.704 4.379 −0.042 1.00 21.23 C ATOM 660C ALA A1087 22.689 6.653 −0.205 1.00 21.63 C ATOM 661 O ALA A1087 23.5087.529 −0.499 1.00 19.21 O ATOM 662 N PRO A1088 21.700 6.872 0.668 1.0020.00 N ATOM 663 CD PRO A1088 20.666 5.919 1.105 1.00 20.94 C ATOM 664CA PRO A1088 21.544 8.164 1.335 1.00 20.18 C ATOM 665 CB PRO A108820.212 8.013 2.064 1.00 20.85 C ATOM 666 CG PRO A1088 20.183 6.545 2.3901.00 22.84 C ATOM 667 C PRO A1088 22.714 8.380 2.281 1.00 19.50 C ATOM668 O PRO A1088 23.220 7.431 2.887 1.00 17.61 O ATOM 669 N TYR A108923.164 9.621 2.395 1.00 18.16 N ATOM 670 CA TYR A1089 24.281 9.913 3.2791.00 19.12 C ATOM 671 CB TYR A1089 25.611 9.642 2.557 1.00 20.66 C ATOM672 CG TYR A1089 25.977 10.698 1.534 1.00 23.33 C ATOM 673 CD1 TYR A108926.869 11.724 1.853 1.00 22.08 C ATOM 674 CE1 TYR A1089 27.211 12.6990.916 1.00 22.82 C ATOM 675 CD2 TYR A1089 25.426 10.673 0.249 1.00 22.30C ATOM 676 CE2 TYR A1089 25.752 11.642 −0.692 1.00 23.44 C ATOM 677 CZTYR A1089 26.649 12.655 −0.354 1.00 25.15 C ATOM 678 OH TYR A1089 26.98713.614 −1.288 1.00 24.63 O ATOM 679 C TYR A1089 24.205 11.363 3.699 1.0017.64 C ATOM 680 O TYR A1089 23.578 12.178 3.023 1.00 16.44 O ATOM 681 NPHE A1090 24.824 11.691 4.825 1.00 17.81 N ATOM 682 CA PHE A1090 24.80113.070 5.277 1.00 17.81 C ATOM 683 CB PHE A1090 25.019 13.159 6.791 1.0017.48 C ATOM 684 CG PHE A1090 23.777 12.873 7.595 1.00 17.01 C ATOM 685CD1 PHE A1090 23.434 11.568 7.938 1.00 17.02 C ATOM 686 CD2 PHE A109022.919 13.910 7.962 1.00 16.23 C ATOM 687 CE1 PHE A1090 22.247 11.2938.632 1.00 17.95 C ATOM 688 CE2 PHE A1090 21.732 13.647 8.656 1.00 17.65C ATOM 689 CZ PHE A1090 21.397 12.333 8.989 1.00 16.73 C ATOM 690 C PHEA1090 25.852 13.892 4.547 1.00 20.29 C ATOM 691 O PHE A1090 27.05413.713 4.749 1.00 19.58 O ATOM 692 N SER A1091 25.384 14.767 3.665 1.0021.20 N ATOM 693 CA SER A1091 26.266 15.646 2.921 1.00 23.08 C ATOM 694CB SER A1091 25.592 16.086 1.618 1.00 24.12 C ATOM 695 OG SER A109124.281 16.567 1.852 1.00 24.36 O ATOM 696 C SER A1091 26.580 16.8563.806 1.00 24.80 C ATOM 697 O SER A1091 27.613 17.507 3.642 1.00 25.24 OATOM 698 N GLN A1092 25.685 17.141 4.752 1.00 24.80 N ATOM 699 CA GLNA1092 25.853 18.254 5.688 1.00 24.09 C ATOM 700 CB GLN A1092 24.97019.448 5.296 1.00 26.54 C ATOM 701 CG GLN A1092 25.294 20.132 3.971 1.0030.86 C ATOM 702 CD GLN A1092 26.711 20.678 3.907 1.00 34.83 C ATOM 703OE1 GLN A1092 27.257 21.147 4.910 1.00 37.27 O ATOM 704 NE2 GLN A109227.308 20.637 2.717 1.00 34.99 N ATOM 705 C GLN A1092 25.453 17.8037.096 1.00 23.97 C ATOM 706 O GLN A1092 24.343 17.295 7.300 1.00 22.36 OATOM 707 N ALA A1093 26.356 17.989 8.057 1.00 20.55 N ATOM 708 CA ALAA1093 26.097 17.621 9.447 1.00 21.00 C ATOM 709 CB ALA A1093 25.94816.101 9.580 1.00 17.57 C ATOM 710 C ALA A1093 27.235 18.114 10.336 1.0022.11 C ATOM 711 O ALA A1093 28.392 18.120 9.920 1.00 23.23 O ATOM 712 NPRO A1094 26.918 18.536 11.573 1.00 23.31 N ATOM 713 CD PRO A1094 25.55018.680 12.111 1.00 23.07 C ATOM 714 CA PRO A1094 27.907 19.034 12.5331.00 24.58 C ATOM 715 CB PRO A1094 27.053 19.820 13.521 1.00 24.45 CATOM 716 CG PRO A1094 25.798 18.997 13.575 1.00 24.77 C ATOM 717 C PROA1094 28.687 17.909 13.219 1.00 26.12 C ATOM 718 O PRO A1094 28.67517.791 14.445 1.00 27.56 O ATOM 719 N PHE A1095 29.353 17.079 12.4231.00 26.05 N ATOM 720 CA PHE A1095 30.139 15.975 12.957 1.00 26.02 CATOM 721 CB PHE A1095 29.279 14.710 13.090 1.00 27.36 C ATOM 722 CG PHEA1095 30.016 13.544 13.674 1.00 26.42 C ATOM 723 CD1 PHE A1095 30.20812.385 12.931 1.00 26.59 C ATOM 724 CD2 PHE A1095 30.571 13.625 14.9501.00 27.10 C ATOM 725 CE1 PHE A1095 30.946 11.324 13.446 1.00 26.29 CATOM 726 CE2 PHE A1095 31.312 12.574 15.475 1.00 25.68 C ATOM 727 CZ PHEA1095 31.502 11.417 14.720 1.00 27.52 C ATOM 728 C PHE A1095 31.30515.727 12.012 1.00 26.40 C ATOM 729 O PHE A1095 31.122 15.681 10.7921.00 25.80 O ATOM 730 N SER A1096 32.498 15.560 12.577 1.00 26.14 N ATOM731 CA SER A1096 33.705 15.357 11.781 1.00 29.05 C ATOM 732 CB SER A109634.909 15.969 12.500 1.00 30.71 C ATOM 733 OG SER A1096 34.768 17.37312.603 1.00 37.13 O ATOM 734 C SER A1096 34.039 13.919 11.413 1.00 28.85C ATOM 735 O SER A1096 34.702 13.678 10.407 1.00 29.54 O ATOM 736 N GLYA1097 33.595 12.968 12.229 1.00 28.58 N ATOM 737 CA GLY A1097 33.88811.573 11.957 1.00 27.16 C ATOM 738 C GLY A1097 32.991 10.948 10.9071.00 26.54 C ATOM 739 O GLY A1097 32.406 11.648 10.077 1.00 27.09 O ATOM740 N LYS A1098 32.888 9.624 10.931 1.00 24.94 N ATOM 741 CA LYS A109832.045 8.930 9.973 1.00 25.69 C ATOM 742 CB LYS A1098 32.587 7.535 9.6441.00 29.36 C ATOM 743 CG LYS A1098 33.687 7.015 10.547 1.00 33.98 C ATOM744 CD LYS A1098 35.051 7.532 10.120 1.00 37.43 C ATOM 745 CE LYS A109836.164 6.583 10.568 1.00 39.11 C ATOM 746 NZ LYS A1098 36.119 6.32012.033 1.00 41.00 N ATOM 747 C LYS A1098 30.625 8.796 10.492 1.00 24.62C ATOM 748 O LYS A1098 30.393 8.494 11.668 1.00 22.63 O ATOM 749 N ILEA1099 29.677 9.033 9.600 1.00 22.17 N ATOM 750 CA ILE A1099 28.273 8.9329.941 1.00 21.57 C ATOM 751 CB ILE A1099 27.514 10.193 9.523 1.00 19.45C ATOM 752 CG2 ILE A1099 26.039 10.056 9.905 1.00 18.01 C ATOM 753 CG1ILE A1099 28.155 11.419 10.177 1.00 20.05 C ATOM 754 CD1 ILE A109927.677 12.738 9.613 1.00 19.45 C ATOM 755 C ILE A1099 27.695 7.748 9.1841.00 21.84 C ATOM 756 O ILE A1099 27.597 7.775 7.958 1.00 24.63 O ATOM757 N TRP A1100 27.334 6.699 9.907 1.00 20.85 N ATOM 758 CA TRP A110026.760 5.532 9.270 1.00 19.86 C ATOM 759 CB TRP A1100 27.172 4.26010.009 1.00 18.86 C ATOM 760 CG TRP A1100 28.652 4.007 9.945 1.00 19.33C ATOM 761 CD2 TRP A1100 29.370 3.395 8.864 1.00 20.59 C ATOM 762 CE2TRP A1100 30.743 3.416 9.209 1.00 20.05 C ATOM 763 CE3 TRP A1100 28.9872.835 7.634 1.00 19.76 C ATOM 764 CD1 TRP A1100 29.590 4.362 10.873 1.0019.35 C ATOM 765 NE1 TRP A1100 30.846 4.010 10.439 1.00 18.87 N ATOM 766CZ2 TRP A1100 31.739 2.895 8.369 1.00 19.48 C ATOM 767 CZ3 TRP A110029.978 2.317 6.796 1.00 22.42 C ATOM 768 CH2 TRP A1100 31.343 2.3547.172 1.00 20.56 C ATOM 769 C TRP A1100 25.251 5.718 9.294 1.00 20.31 CATOM 770 O TRP A1100 24.633 5.795 10.357 1.00 20.18 O ATOM 771 N LEUA1101 24.663 5.829 8.113 1.00 18.06 N ATOM 772 CA LEU A1101 23.229 6.0238.019 1.00 17.46 C ATOM 773 CB LEU A1101 22.915 7.399 7.409 1.00 15.91 CATOM 774 CG LEU A1101 21.475 7.611 6.919 1.00 15.54 C ATOM 775 CD1 LEUA1101 20.510 7.621 8.101 1.00 14.01 C ATOM 776 CD2 LEU A1101 21.3808.931 6.150 1.00 12.69 C ATOM 777 C LEU A1101 22.561 4.945 7.190 1.0017.42 C ATOM 778 O LEU A1101 23.124 4.436 6.218 1.00 15.25 O ATOM 779 NSER A1102 21.353 4.582 7.600 1.00 17.54 N ATOM 780 CA SER A1102 20.5813.607 6.865 1.00 15.75 C ATOM 781 CB SER A1102 20.832 2.189 7.364 1.0016.41 C ATOM 782 OG SER A1102 20.242 1.258 6.469 1.00 14.51 O ATOM 783 CSER A1102 19.129 3.980 7.063 1.00 17.48 C ATOM 784 O SER A1102 18.7114.322 8.173 1.00 16.20 O ATOM 785 N ILE A1103 18.376 3.940 5.968 1.0017.02 N ATOM 786 CA ILE A1103 16.963 4.274 5.979 1.00 17.85 C ATOM 787CB ILE A1103 16.691 5.576 5.194 1.00 19.00 C ATOM 788 CG2 ILE A110315.207 5.948 5.278 1.00 18.57 C ATOM 789 CG1 ILE A1103 17.554 6.7065.754 1.00 18.22 C ATOM 790 CD1 ILE A1103 17.414 8.014 4.999 1.00 20.97C ATOM 791 C ILE A1103 16.239 3.130 5.291 1.00 17.46 C ATOM 792 O ILEA1103 16.769 2.510 4.368 1.00 17.27 O ATOM 793 N SER A1104 15.033 2.8455.751 1.00 14.92 N ATOM 794 CA SER A1104 14.240 1.772 5.175 1.00 17.06 CATOM 795 CB SER A1104 14.566 0.447 5.876 1.00 15.94 C ATOM 796 OG SERA1104 13.790 −0.613 5.342 1.00 15.77 O ATOM 797 C SER A1104 12.779 2.1555.384 1.00 17.20 C ATOM 798 O SER A1104 12.453 2.859 6.333 1.00 15.90 OATOM 799 N HIS A1105 11.902 1.699 4.502 1.00 18.52 N ATOM 800 CA HISA1105 10.494 2.048 4.619 1.00 20.22 C ATOM 801 CB HIS A1105 10.199 3.3163.813 1.00 23.50 C ATOM 802 CG HIS A1105 10.358 3.127 2.334 1.00 25.77 CATOM 803 CD2 HIS A1105 9.487 2.690 1.392 1.00 26.90 C ATOM 804 ND1 HISA1105 11.563 3.301 1.687 1.00 26.39 N ATOM 805 CE1 HIS A1105 11.4282.977 0.412 1.00 27.48 C ATOM 806 NE2 HIS A1105 10.177 2.601 0.208 1.0027.67 N ATOM 807 C HIS A1105 9.597 0.953 4.079 1.00 21.15 C ATOM 808 OHIS A1105 10.054 0.040 3.392 1.00 21.16 O ATOM 809 N THR A1106 8.3131.067 4.402 1.00 21.46 N ATOM 810 CA THR A1106 7.290 0.160 3.911 1.0022.28 C ATOM 811 CB THR A1106 6.646 −0.682 5.032 1.00 21.51 C ATOM 812OG1 THR A1106 5.891 0.169 5.904 1.00 19.68 O ATOM 813 CG2 THR A11067.716 −1.415 5.827 1.00 21.79 C ATOM 814 C THR A1106 6.263 1.161 3.3861.00 24.40 C ATOM 815 O THR A1106 6.560 2.356 3.309 1.00 22.60 O ATOM816 N ASP A1107 5.070 0.698 3.032 1.00 25.68 N ATOM 817 CA ASP A11074.050 1.612 2.534 1.00 28.90 C ATOM 818 CB ASP A1107 2.952 0.845 1.7871.00 34.46 C ATOM 819 CG ASP A1107 3.479 0.098 0.574 1.00 40.33 C ATOM820 OD1 ASP A1107 4.229 0.704 −0.225 1.00 43.51 O ATOM 821 OD2 ASP A11073.134 −1.093 0.413 1.00 43.99 O ATOM 822 C ASP A1107 3.420 2.385 3.6911.00 28.81 C ATOM 823 O ASP A1107 2.613 3.285 3.470 1.00 29.78 O ATOM824 N GLN A1108 3.801 2.049 4.921 1.00 25.83 N ATOM 825 CA GLN A11083.228 2.710 6.086 1.00 24.71 C ATOM 826 CB GLN A1108 2.384 1.710 6.8671.00 27.32 C ATOM 827 CG GLN A1108 1.328 1.026 6.030 1.00 32.60 C ATOM828 CD GLN A1108 0.951 −0.324 6.583 1.00 35.93 C ATOM 829 OE1 GLN A11081.085 −1.344 5.902 1.00 37.52 O ATOM 830 NE2 GLN A1108 0.481 −0.3467.829 1.00 36.07 N ATOM 831 C GLN A1108 4.224 3.356 7.038 1.00 24.10 CATOM 832 O GLN A1108 3.879 4.305 7.742 1.00 23.70 O ATOM 833 N PHE A11095.448 2.840 7.082 1.00 22.72 N ATOM 834 CA PHE A1109 6.452 3.389 7.9831.00 21.31 C ATOM 835 CB PHE A1109 6.719 2.446 9.164 1.00 22.89 C ATOM836 CG PHE A1109 5.518 2.151 10.004 1.00 25.18 C ATOM 837 CD1 PHE A11094.746 1.018 9.763 1.00 26.55 C ATOM 838 CD2 PHE A1109 5.155 3.003 11.0441.00 26.19 C ATOM 839 CE1 PHE A1109 3.626 0.734 10.549 1.00 26.78 C ATOM840 CE2 PHE A1109 4.037 2.729 11.834 1.00 26.65 C ATOM 841 CZ PHE A11093.273 1.591 11.584 1.00 25.88 C ATOM 842 C PHE A1109 7.785 3.630 7.3181.00 20.22 C ATOM 843 O PHE A1109 8.096 3.053 6.275 1.00 19.27 O ATOM844 N VAL A1110 8.573 4.489 7.951 1.00 18.43 N ATOM 845 CA VAL A11109.925 4.781 7.507 1.00 19.10 C ATOM 846 CB VAL A1110 10.049 6.191 6.8461.00 19.04 C ATOM 847 CG1 VAL A1110 9.654 7.277 7.820 1.00 19.30 C ATOM848 CG2 VAL A1110 11.474 6.412 6.359 1.00 23.53 C ATOM 849 C VAL A111010.744 4.718 8.797 1.00 19.12 C ATOM 850 O VAL A1110 10.287 5.169 9.8541.00 17.72 O ATOM 851 N THR A1111 11.925 4.115 8.720 1.00 18.67 N ATOM852 CA THR A1111 12.805 3.992 9.875 1.00 20.42 C ATOM 853 CB THR A111112.897 2.525 10.397 1.00 22.98 C ATOM 854 OG1 THR A1111 13.363 1.6709.345 1.00 25.86 O ATOM 855 CG2 THR A1111 11.548 2.029 10.874 1.00 24.99C ATOM 856 C THR A1111 14.200 4.421 9.456 1.00 20.11 C ATOM 857 O THRA1111 14.575 4.287 8.291 1.00 20.53 O ATOM 858 N ALA A1112 14.962 4.94610.404 1.00 17.15 N ATOM 859 CA ALA A1112 16.321 5.370 10.119 1.00 18.28C ATOM 860 CB ALA A1112 16.357 6.858 9.791 1.00 16.81 C ATOM 861 C ALAA1112 17.190 5.080 11.328 1.00 18.04 C ATOM 862 O ALA A1112 16.721 5.14212.464 1.00 17.37 O ATOM 863 N SER A1113 18.454 4.755 11.075 1.00 17.48N ATOM 864 CA SER A1113 19.401 4.479 12.146 1.00 17.23 C ATOM 865 CB SERA1113 19.635 2.967 12.283 1.00 15.09 C ATOM 866 OG SER A1113 20.6662.686 13.224 1.00 16.24 O ATOM 867 C SER A1113 20.718 5.187 11.844 1.0017.94 C ATOM 868 O SER A1113 21.209 5.158 10.712 1.00 18.05 O ATOM 869 NVAL A1114 21.285 5.832 12.857 1.00 18.42 N ATOM 870 CA VAL A1114 22.5466.543 12.683 1.00 17.97 C ATOM 871 CB VAL A1114 22.350 8.082 12.783 1.0017.35 C ATOM 872 CG1 VAL A1114 23.708 8.784 12.874 1.00 15.58 C ATOM 873CG2 VAL A1114 21.571 8.592 11.571 1.00 16.65 C ATOM 874 C VAL A111423.565 6.130 13.735 1.00 18.00 C ATOM 875 O VAL A1114 23.241 6.02314.926 1.00 17.56 O ATOM 876 N ILE A1115 24.793 5.885 13.286 1.00 17.57N ATOM 877 CA ILE A1115 25.885 5.536 14.181 1.00 15.61 C ATOM 878 CB ILEA1115 26.416 4.109 13.951 1.00 17.48 C ATOM 879 CG2 ILE A1115 27.5143.806 14.965 1.00 14.97 C ATOM 880 CG1 ILE A1115 25.287 3.086 14.0821.00 16.92 C ATOM 881 CD1 ILE A1115 25.695 1.685 13.638 1.00 16.69 CATOM 882 C ILE A1115 27.019 6.499 13.860 1.00 17.74 C ATOM 883 O ILEA1115 27.470 6.573 12.714 1.00 16.21 O ATOM 884 N LEU A1116 27.470 7.24614.864 1.00 17.78 N ATOM 885 CA LEU A1116 28.562 8.188 14.668 1.00 19.32C ATOM 886 CB LEU A1116 28.333 9.442 15.510 1.00 20.38 C ATOM 887 CG LEUA1116 26.963 10.095 15.322 1.00 20.47 C ATOM 888 CD1 LEU A1116 26.87711.326 16.205 1.00 22.94 C ATOM 889 CD2 LEU A1116 26.751 10.462 13.8601.00 18.60 C ATOM 890 C LEU A1116 29.851 7.490 15.093 1.00 21.10 C ATOM891 O LEU A1116 29.909 6.870 16.156 1.00 19.16 O ATOM 892 N GLU A111730.880 7.590 14.259 1.00 22.54 N ATOM 893 CA GLU A1117 32.141 6.93414.554 1.00 25.40 C ATOM 894 CB GLU A1117 32.323 5.743 13.616 1.00 25.16C ATOM 895 CG GLU A1117 33.629 5.000 13.817 1.00 27.61 C ATOM 896 CD GLUA1117 33.720 3.772 12.950 1.00 27.04 C ATOM 897 OE1 GLU A1117 33.3913.875 11.750 1.00 27.90 O ATOM 898 OE2 GLU A1117 34.126 2.712 13.4651.00 27.49 O ATOM 899 C GLU A1117 33.358 7.852 14.464 1.00 27.82 C ATOM900 O GLU A1117 33.425 8.742 13.616 1.00 26.44 O ATOM 901 N GLU A111834.328 7.605 15.339 1.00 31.38 N ATOM 902 CA GLU A1118 35.549 8.39615.387 1.00 35.38 C ATOM 903 CB GLU A1118 35.632 9.122 16.732 1.00 38.96C ATOM 904 CG GLU A1118 36.450 10.397 16.711 1.00 44.28 C ATOM 905 CDGLU A1118 35.953 11.381 15.671 1.00 46.94 C ATOM 906 OE1 GLU A111836.206 11.153 14.469 1.00 47.99 O ATOM 907 OE2 GLU A1118 35.302 12.37716.054 1.00 49.20 O ATOM 908 C GLU A1118 36.756 7.482 15.210 1.00 36.85C ATOM 909 O GLU A1118 37.586 7.767 14.319 1.00 39.18 O ATOM 910 OXT GLUA1118 36.858 6.488 15.967 1.00 37.85 O TER 911 GLU A1118 ATOM 912 CB METB2003 36.089 −4.001 20.131 1.00 36.93 C ATOM 913 CG MET B2003 35.997−4.450 21.581 1.00 42.07 C ATOM 914 SD MET B2003 37.062 −5.865 21.9641.00 49.34 S ATOM 915 CE MET B2003 36.267 −7.158 21.006 1.00 46.76 CATOM 916 C MET B2003 33.796 −3.017 20.233 1.00 31.67 C ATOM 917 O METB2003 33.469 −2.921 21.422 1.00 28.54 O ATOM 918 N MET B2003 35.809−1.560 20.439 1.00 33.64 N ATOM 919 CA MET B2003 35.239 −2.773 19.7911.00 33.04 C ATOM 920 N ILE B2004 32.938 −3.327 19.264 1.00 29.22 N ATOM921 CA ILE B2004 31.537 −3.604 19.538 1.00 26.95 C ATOM 922 CB ILE B200430.694 −3.586 18.236 1.00 27.19 C ATOM 923 CG2 ILE B2004 29.273 −4.07018.528 1.00 26.67 C ATOM 924 CG1 ILE B2004 30.692 −2.175 17.642 1.0027.75 C ATOM 925 CD1 ILE B2004 29.965 −2.048 16.307 1.00 28.82 C ATOM926 C ILE B2004 31.452 −4.986 20.165 1.00 25.64 C ATOM 927 O ILE B200432.092 −5.924 19.693 1.00 26.78 O ATOM 928 N VAL B2005 30.681 −5.11421.240 1.00 23.42 N ATOM 929 CA VAL B2005 30.534 −6.406 21.904 1.0022.67 C ATOM 930 CB VAL B2005 31.099 −6.379 23.344 1.00 23.16 C ATOM 931CG1 VAL B2005 32.615 −6.311 23.305 1.00 22.80 C ATOM 932 CG2 VAL B200530.552 −5.197 24.096 1.00 23.38 C ATOM 933 C VAL B2005 29.086 −6.87821.948 1.00 21.18 C ATOM 934 O VAL B2005 28.772 −7.884 22.577 1.00 23.33O ATOM 935 N GLY B2006 28.200 −6.155 21.275 1.00 19.21 N ATOM 936 CA GLYB2006 26.811 −6.568 21.260 1.00 17.80 C ATOM 937 C GLY B2006 25.896−5.584 20.567 1.00 17.03 C ATOM 938 O GLY B2006 26.161 −4.387 20.5531.00 16.68 O ATOM 939 N HIS B2007 24.813 −6.093 19.989 1.00 16.35 N ATOM940 CA HIS B2007 23.846 −5.237 19.323 1.00 16.88 C ATOM 941 CB HIS B200724.216 −5.042 17.847 1.00 17.35 C ATOM 942 CG HIS B2007 23.254 −4.17017.097 1.00 18.35 C ATOM 943 CD2 HIS B2007 22.786 −4.239 15.827 1.0017.84 C ATOM 944 ND1 HIS B2007 22.668 −3.058 17.660 1.00 18.04 N ATOM945 CE1 HIS B2007 21.880 −2.479 16.769 1.00 19.69 C ATOM 946 NE2 HISB2007 21.934 −3.176 15.648 1.00 16.84 N ATOM 947 C HIS B2007 22.447−5.831 19.444 1.00 17.26 C ATOM 948 O HIS B2007 22.238 −7.027 19.2131.00 14.74 O ATOM 949 N GLY B2008 21.490 −4.990 19.819 1.00 16.95 N ATOM950 CA GLY B2008 20.129 −5.464 19.962 1.00 17.68 C ATOM 951 C GLY B200819.095 −4.401 19.661 1.00 18.32 C ATOM 952 O GLY B2008 19.321 −3.21219.901 1.00 19.75 O ATOM 953 N ILE B2009 17.964 −4.830 19.112 1.00 17.31N ATOM 954 CA ILE B2009 16.868 −3.917 18.821 1.00 18.07 C ATOM 955 CBILE B2009 16.727 −3.598 17.306 1.00 16.33 C ATOM 956 CG2 ILE B200918.025 −2.990 16.777 1.00 16.15 C ATOM 957 CG1 ILE B2009 16.361 −4.85616.519 1.00 19.06 C ATOM 958 CD1 ILE B2009 16.014 −4.559 15.060 1.0016.01 C ATOM 959 C ILE B2009 15.607 −4.607 19.312 1.00 17.52 C ATOM 960O ILE B2009 15.576 −5.827 19.448 1.00 17.73 O ATOM 961 N ASP B201014.580 −3.825 19.607 1.00 18.54 N ATOM 962 CA ASP B2010 13.327 −4.38420.089 1.00 20.76 C ATOM 963 CB ASP B2010 13.401 −4.663 21.598 1.0021.38 C ATOM 964 CG ASP B2010 12.157 −5.372 22.127 1.00 22.62 C ATOM 965OD1 ASP B2010 11.403 −4.762 22.915 1.00 22.62 O ATOM 966 OD2 ASP B201011.932 −6.544 21.756 1.00 23.17 O ATOM 967 C ASP B2010 12.198 −3.41619.814 1.00 21.83 C ATOM 968 O ASP B2010 12.378 −2.200 19.912 1.00 21.02O ATOM 969 N ILE B2011 11.039 −3.966 19.464 1.00 21.90 N ATOM 970 CA ILEB2011 9.848 −3.163 19.189 1.00 25.52 C ATOM 971 CB ILE B2011 9.346−3.346 17.752 1.00 27.88 C ATOM 972 CG2 ILE B2011 8.410 −2.194 17.3881.00 30.28 C ATOM 973 CG1 ILE B2011 10.518 −3.410 16.783 1.00 29.66 CATOM 974 CD1 ILE B2011 10.131 −3.937 15.420 1.00 31.53 C ATOM 975 C ILEB2011 8.738 −3.670 20.102 1.00 24.08 C ATOM 976 O ILE B2011 8.561 −4.87420.258 1.00 22.40 O ATOM 977 N GLU B2012 8.002 −2.757 20.718 1.00 24.39N ATOM 978 CA GLU B2012 6.911 −3.156 21.598 1.00 24.77 C ATOM 979 CB GLUB2012 7.269 −2.868 23.056 1.00 25.42 C ATOM 980 CG GLU B2012 8.482−3.637 23.554 1.00 28.89 C ATOM 981 CD GLU B2012 8.233 −5.139 23.6521.00 31.05 C ATOM 982 OE1 GLU B2012 9.224 −5.895 23.721 1.00 31.07 OATOM 983 OE2 GLU B2012 7.053 −5.560 23.671 1.00 30.63 O ATOM 984 C GLUB2012 5.655 −2.387 21.208 1.00 24.28 C ATOM 985 O GLU B2012 5.732 −1.23520.786 1.00 24.45 O ATOM 986 N GLU B2013 4.507 −3.043 21.328 1.00 22.06N ATOM 987 CA GLU B2013 3.223 −2.431 21.008 1.00 21.01 C ATOM 988 CB GLUB2013 2.241 −3.508 20.545 1.00 21.98 C ATOM 989 CG GLU B2013 0.857−3.010 20.179 0.05 20.80 C ATOM 990 CD GLU B2013 −0.106 −4.152 19.9210.05 20.56 C ATOM 991 OE1 GLU B2013 0.231 −5.039 19.109 0.05 20.26 OATOM 992 OE2 GLU B2013 −1.196 −4.166 20.529 0.05 20.00 O ATOM 993 C GLUB2013 2.719 −1.793 22.292 1.00 20.42 C ATOM 994 O GLU B2013 2.644 −2.45723.326 1.00 19.82 O ATOM 995 N LEU B2014 2.383 −0.512 22.244 1.00 20.95N ATOM 996 CA LEU B2014 1.906 0.149 23.452 1.00 25.05 C ATOM 997 CB LEUB2014 1.530 1.604 23.162 1.00 26.46 C ATOM 998 CG LEU B2014 2.610 2.47822.521 1.00 29.15 C ATOM 999 CD1 LEU B2014 2.171 3.929 22.610 1.00 32.28C ATOM 1000 CD2 LEU B2014 3.945 2.294 23.225 1.00 28.39 C ATOM 1001 CLEU B2014 0.708 −0.582 24.053 1.00 25.52 C ATOM 1002 O LEU B2014 0.635−0.773 25.266 1.00 25.48 O ATOM 1003 N ALA B2015 −0.220 −1.001 23.1961.00 26.92 N ATOM 1004 CA ALA B2015 −1.425 −1.697 23.637 1.00 28.21 CATOM 1005 CB ALA B2015 −2.267 −2.088 22.426 1.00 29.71 C ATOM 1006 C ALAB2015 −1.144 −2.932 24.490 1.00 29.10 C ATOM 1007 O ALA B2015 −1.864−3.208 25.450 1.00 29.79 O ATOM 1008 N SER B2016 −0.106 −3.681 24.1351.00 29.36 N ATOM 1009 CA SER B2016 0.246 −4.885 24.875 1.00 30.31 CATOM 1010 CB SER B2016 1.357 −5.633 24.147 1.00 32.28 C ATOM 1011 OG SERB2016 1.032 −5.782 22.779 1.00 33.64 O ATOM 1012 C SER B2016 0.705−4.508 26.275 1.00 30.37 C ATOM 1013 O SER B2016 0.369 −5.170 27.2601.00 29.37 O ATOM 1014 N ILE B2017 1.476 −3.431 26.353 1.00 30.04 N ATOM1015 CA ILE B2017 1.979 −2.955 27.625 1.00 30.17 C ATOM 1016 CB ILEB2017 2.907 −1.741 27.420 1.00 29.67 C ATOM 1017 CG2 ILE B2017 3.323−1.153 28.765 1.00 31.54 C ATOM 1018 CG1 ILE B2017 4.141 −2.178 26.6301.00 29.63 C ATOM 1019 CD1 ILE B2017 4.883 −3.368 27.246 1.00 29.53 CATOM 1020 C ILE B2017 0.814 −2.585 28.537 1.00 30.53 C ATOM 1021 O ILEB2017 0.736 −3.051 29.673 1.00 29.90 O ATOM 1022 N GLU B2018 −0.100−1.762 28.034 1.00 31.91 N ATOM 1023 CA GLU B2018 −1.252 −1.363 28.8311.00 34.92 C ATOM 1024 CB GLU B2018 −2.113 −0.355 28.064 1.00 37.97 CATOM 1025 CG GLU B2018 −1.895 −0.370 26.565 1.00 42.86 C ATOM 1026 CDGLU B2018 −2.698 0.700 25.844 1.00 45.97 C ATOM 1027 OE1 GLU B2018−3.945 0.608 25.843 1.00 47.86 O ATOM 1028 OE2 GLU B2018 −2.084 1.63325.279 1.00 47.02 O ATOM 1029 C GLU B2018 −2.085 −2.573 29.247 1.0034.56 C ATOM 1030 O GLU B2018 −2.490 −2.678 30.404 1.00 35.89 O ATOM1031 N SER B2019 −2.349 −3.488 28.321 1.00 33.29 N ATOM 1032 CA SERB2019 −3.117 −4.674 28.681 1.00 33.75 C ATOM 1033 CB SER B2019 −3.270−5.623 27.490 1.00 32.73 C ATOM 1034 OG SER B2019 −4.314 −5.203 26.6351.00 36.89 O ATOM 1035 C SER B2019 −2.416 −5.402 29.822 1.00 33.12 CATOM 1036 O SER B2019 −3.066 −5.963 30.698 1.00 32.83 O ATOM 1037 N ALAB2020 −1.087 −5.398 29.808 1.00 33.22 N ATOM 1038 CA ALA B2020 −0.329−6.055 30.869 1.00 35.36 C ATOM 1039 CB ALA B2020 1.157 −6.105 30.5101.00 34.87 C ATOM 1040 C ALA B2020 −0.537 −5.295 32.179 1.00 36.08 CATOM 1041 O ALA B2020 −0.669 −5.898 33.241 1.00 34.70 O ATOM 1042 N VALB2021 −0.570 −3.968 32.097 1.00 38.89 N ATOM 1043 CA VAL B2021 −0.783−3.133 33.277 1.00 42.15 C ATOM 1044 CB VAL B2021 −0.672 −1.627 32.9311.00 42.05 C ATOM 1045 CG1 VAL B2021 −1.060 −0.775 34.138 1.00 42.48 CATOM 1046 CG2 VAL B2021 0.746 −1.298 32.504 1.00 42.42 C ATOM 1047 C VALB2021 −2.176 −3.410 33.841 1.00 44.98 C ATOM 1048 O VAL B2021 −2.491−3.029 34.967 1.00 45.67 O ATOM 1049 N THR B2022 −3.001 −4.085 33.0471.00 47.50 N ATOM 1050 CA THR B2022 −4.359 −4.420 33.451 1.00 50.10 CATOM 1051 CB THR B2022 −5.323 −4.368 32.236 1.00 51.16 C ATOM 1052 OG1THR B2022 −5.501 −3.007 31.824 1.00 53.24 O ATOM 1053 CG2 THR B2022−6.677 −4.957 32.592 1.00 52.95 C ATOM 1054 C THR B2022 −4.454 −5.79934.109 1.00 50.81 C ATOM 1055 O THR B2022 −4.937 −5.918 35.232 1.0051.36 O ATOM 1056 N ARG B2023 −3.988 −6.836 33.421 1.00 51.25 N ATOM1057 CA ARG B2023 −4.064 −8.187 33.968 1.00 52.22 C ATOM 1058 CB ARGB2023 −3.746 −9.220 32.883 1.00 52.29 C ATOM 1059 CG ARG B2023 −4.157−10.644 33.242 0.05 51.97 C ATOM 1060 CD ARG B2023 −5.531 −10.663 33.9050.05 51.83 C ATOM 1061 NE ARG B2023 −6.183 −11.966 33.828 0.05 51.66 NATOM 1062 CZ ARG B2023 −6.697 −12.474 32.713 0.05 51.57 C ATOM 1063 NH1ARG B2023 −6.634 −11.789 31.579 0.05 51.47 N ATOM 1064 NH2 ARG B2023−7.284 −13.663 32.730 0.05 51.49 N ATOM 1065 C ARG B2023 −3.157 −8.40535.173 1.00 53.22 C ATOM 1066 O ARG B2023 −3.256 −9.424 35.859 1.0053.07 O ATOM 1067 N HIS B2024 −2.274 −7.447 35.432 1.00 53.34 N ATOM1068 CA HIS B2024 −1.365 −7.544 36.564 1.00 53.62 C ATOM 1069 CB HISB2024 −0.042 −8.176 36.127 1.00 54.97 C ATOM 1070 CG HIS B2024 −0.208−9.477 35.403 1.00 56.91 C ATOM 1071 CD2 HIS B2024 −0.006 −10.755 35.8051.00 57.80 C ATOM 1072 ND1 HIS B2024 −0.660 −9.552 34.103 1.00 57.75 NATOM 1073 CE1 HIS B2024 −0.729 −10.820 33.735 1.00 58.06 C ATOM 1074 NE2HIS B2024 −0.338 −11.570 34.750 1.00 57.59 N ATOM 1075 C HIS B2024−1.127 −6.157 37.148 1.00 53.35 C ATOM 1076 O HIS B2024 −0.312 −5.38536.644 1.00 53.29 O ATOM 1077 N GLU B2025 −1.861 −5.854 38.214 1.0052.80 N ATOM 1078 CA GLU B2025 −1.785 −4.569 38.905 1.00 51.46 C ATOM1079 CB GLU B2025 −2.618 −4.637 40.188 1.00 54.49 C ATOM 1080 CG GLUB2025 −4.095 −4.920 39.949 1.00 56.85 C ATOM 1081 CD GLU B2025 −4.798−5.434 41.190 1.00 58.84 C ATOM 1082 OE1 GLU B2025 −4.520 −6.584 41.5951.00 60.08 O ATOM 1083 OE2 GLU B2025 −5.624 −4.690 41.763 1.00 59.42 OATOM 1084 C GLU B2025 −0.364 −4.122 39.247 1.00 48.83 C ATOM 1085 O GLUB2025 −0.058 −2.931 39.211 1.00 48.34 O ATOM 1086 N GLY B2026 0.497−5.074 39.588 1.00 45.49 N ATOM 1087 CA GLY B2026 1.864 −4.729 39.9321.00 40.95 C ATOM 1088 C GLY B2026 2.826 −4.920 38.774 1.00 37.63 C ATOM1089 O GLY B2026 4.027 −5.077 38.978 1.00 37.06 O ATOM 1090 N PHE B20272.301 −4.902 37.554 1.00 33.22 N ATOM 1091 CA PHE B2027 3.135 −5.08336.374 1.00 30.35 C ATOM 1092 CB PHE B2027 2.287 −4.995 35.105 1.0029.47 C ATOM 1093 CG PHE B2027 3.079 −5.162 33.840 1.00 28.37 C ATOM1094 CD1 PHE B2027 3.501 −6.421 33.431 1.00 28.75 C ATOM 1095 CD2 PHEB2027 3.432 −4.055 33.076 1.00 26.82 C ATOM 1096 CE1 PHE B2027 4.264−6.575 32.277 1.00 27.85 C ATOM 1097 CE2 PHE B2027 4.195 −4.199 31.9191.00 27.50 C ATOM 1098 CZ PHE B2027 4.611 −5.458 31.520 1.00 28.11 CATOM 1099 C PHE B2027 4.245 −4.038 36.303 1.00 28.35 C ATOM 1100 O PHEB2027 5.419 −4.378 36.179 1.00 27.55 O ATOM 1101 N ALA B2028 3.863−2.768 36.376 1.00 26.54 N ATOM 1102 CA ALA B2028 4.820 −1.674 36.3061.00 26.97 C ATOM 1103 CB ALA B2028 4.103 −0.340 36.503 1.00 26.06 CATOM 1104 C ALA B2028 5.938 −1.815 37.329 1.00 27.20 C ATOM 1105 O ALAB2028 7.112 −1.697 36.998 1.00 26.33 O ATOM 1106 N LYS B2029 5.555−2.075 38.572 1.00 28.14 N ATOM 1107 CA LYS B2029 6.496 −2.213 39.6731.00 30.24 C ATOM 1108 CB LYS B2029 5.738 −2.543 40.965 1.00 33.94 CATOM 1109 CG LYS B2029 6.597 −2.502 42.215 1.00 39.10 C ATOM 1110 CD LYSB2029 7.038 −1.082 42.540 1.00 42.39 C ATOM 1111 CE LYS B2029 8.108−1.070 43.629 1.00 45.14 C ATOM 1112 NZ LYS B2029 7.712 −1.858 44.8361.00 46.16 N ATOM 1113 C LYS B2029 7.567 −3.264 39.437 1.00 28.56 C ATOM1114 O LYS B2029 8.696 −3.114 39.902 1.00 28.42 O ATOM 1115 N ARG B20307.219 −4.325 38.717 1.00 26.96 N ATOM 1116 CA ARG B2030 8.171 −5.39738.452 1.00 25.76 C ATOM 1117 CB ARG B2030 7.430 −6.708 38.180 1.0027.87 C ATOM 1118 CG ARG B2030 6.318 −7.007 39.174 0.05 26.73 C ATOM1119 CD ARG B2030 6.358 −8.451 39.652 0.05 26.68 C ATOM 1120 NE ARGB2030 6.295 −9.416 38.557 0.05 26.45 N ATOM 1121 CZ ARG B2030 5.263−9.553 37.730 0.05 26.36 C ATOM 1122 NH1 ARG B2030 4.191 −8.783 37.8620.05 26.22 N ATOM 1123 NH2 ARG B2030 5.301 −10.469 36.771 0.05 26.29 NATOM 1124 C ARG B2030 9.069 −5.076 37.266 1.00 24.16 C ATOM 1125 O ARGB2030 10.200 −5.551 37.187 1.00 22.83 O ATOM 1126 N VAL B2031 8.559−4.270 36.341 1.00 22.75 N ATOM 1127 CA VAL B2031 9.319 −3.903 35.1581.00 22.54 C ATOM 1128 CB VAL B2031 8.371 −3.536 33.984 1.00 23.94 CATOM 1129 CG1 VAL B2031 9.156 −2.884 32.855 1.00 24.54 C ATOM 1130 CG2VAL B2031 7.677 −4.794 33.467 1.00 24.38 C ATOM 1131 C VAL B2031 10.264−2.739 35.409 1.00 21.20 C ATOM 1132 O VAL B2031 11.364 −2.699 34.8581.00 21.89 O ATOM 1133 N LEU B2032 9.837 −1.805 36.252 1.00 20.43 N ATOM1134 CA LEU B2032 10.623 −0.607 36.552 1.00 21.46 C ATOM 1135 CB LEUB2032 9.722 0.624 36.459 1.00 21.16 C ATOM 1136 CG LEU B2032 8.902 0.81435.180 1.00 22.44 C ATOM 1137 CD1 LEU B2032 7.913 1.951 35.383 1.0025.05 C ATOM 1138 CD2 LEU B2032 9.822 1.107 34.003 1.00 23.51 C ATOM1139 C LEU B2032 11.289 −0.613 37.928 1.00 20.88 C ATOM 1140 O LEU B203210.758 −1.188 38.875 1.00 24.06 O ATOM 1141 N THR B2033 12.451 0.02738.035 1.00 20.86 N ATOM 1142 CA THR B2033 13.147 0.117 39.317 1.0020.81 C ATOM 1143 CB THR B2033 14.602 0.569 39.160 1.00 20.39 C ATOM1144 OG1 THR B2033 14.623 1.853 38.521 1.00 21.21 O ATOM 1145 CG2 THRB2033 15.394 −0.443 38.341 1.00 20.57 C ATOM 1146 C THR B2033 12.4321.189 40.119 1.00 21.74 C ATOM 1147 O THR B2033 11.479 1.806 39.635 1.0022.52 O ATOM 1148 N ALA B2034 12.893 1.427 41.339 1.00 22.64 N ATOM 1149CA ALA B2034 12.267 2.441 42.177 1.00 24.18 C ATOM 1150 CB ALA B203412.939 2.479 43.541 1.00 24.55 C ATOM 1151 C ALA B2034 12.371 3.80641.502 1.00 25.08 C ATOM 1152 O ALA B2034 11.393 4.555 41.437 1.00 24.57O ATOM 1153 N LEU B2035 13.558 4.119 40.989 1.00 25.67 N ATOM 1154 CALEU B2035 13.786 5.403 40.337 1.00 27.37 C ATOM 1155 CB LEU B2035 15.2745.576 40.025 1.00 30.75 C ATOM 1156 CG LEU B2035 15.792 7.017 40.0161.00 34.25 C ATOM 1157 CD1 LEU B2035 15.529 7.681 41.373 1.00 34.25 CATOM 1158 CD2 LEU B2035 17.286 7.010 39.715 1.00 36.03 C ATOM 1159 C LEUB2035 12.948 5.550 39.066 1.00 26.19 C ATOM 1160 O LEU B2035 12.4246.625 38.789 1.00 25.81 O ATOM 1161 N GLU B2036 12.829 4.479 38.288 1.0024.86 N ATOM 1162 CA GLU B2036 12.010 4.523 37.074 1.00 24.94 C ATOM1163 CB GLU B2036 12.218 3.256 36.238 1.00 24.20 C ATOM 1164 CG GLUB2036 13.521 3.220 35.439 1.00 22.34 C ATOM 1165 CD GLU B2036 13.8231.834 34.878 1.00 22.43 C ATOM 1166 OE1 GLU B2036 14.592 1.744 33.8991.00 20.15 O ATOM 1167 OE2 GLU B2036 13.302 0.834 35.425 1.00 21.31 OATOM 1168 C GLU B2036 10.528 4.645 37.461 1.00 25.14 C ATOM 1169 O GLUB2036 9.740 5.261 36.746 1.00 24.49 O ATOM 1170 N MET B2037 10.155 4.05138.593 1.00 25.36 N ATOM 1171 CA MET B2037 8.772 4.116 39.067 1.00 27.03C ATOM 1172 CB MET B2037 8.570 3.202 40.279 1.00 28.19 C ATOM 1173 CGMET B2037 8.077 1.811 39.932 1.00 30.50 C ATOM 1174 SD MET B2037 6.5921.878 38.903 1.00 35.36 S ATOM 1175 CE MET B2037 5.315 2.130 40.111 1.0031.11 C ATOM 1176 C MET B2037 8.389 5.541 39.445 1.00 27.51 C ATOM 1177O MET B2037 7.288 6.004 39.146 1.00 27.72 O ATOM 1178 N GLU B2038 9.3096.232 40.104 1.00 29.26 N ATOM 1179 CA GLU B2038 9.075 7.604 40.522 1.0030.50 C ATOM 1180 CB GLU B2038 10.261 8.089 41.363 1.00 33.66 C ATOM1181 CG GLU B2038 10.100 7.747 42.852 1.00 38.27 C ATOM 1182 CD GLUB2038 11.384 7.278 43.517 1.00 41.20 C ATOM 1183 OE1 GLU B2038 12.4487.886 43.264 1.00 41.95 O ATOM 1184 OE2 GLU B2038 11.322 6.307 44.3091.00 42.56 O ATOM 1185 C GLU B2038 8.827 8.512 39.320 1.00 29.98 C ATOM1186 O GLU B2038 8.059 9.473 39.403 1.00 29.40 O ATOM 1187 N ARG B20399.465 8.198 38.198 1.00 28.37 N ATOM 1188 CA ARG B2039 9.272 8.97336.986 1.00 28.60 C ATOM 1189 CB ARG B2039 10.374 8.670 35.973 1.0032.59 C ATOM 1190 CG ARG B2039 10.103 9.236 34.589 1.00 36.59 C ATOM1191 CD ARG B2039 9.892 10.740 34.627 1.00 42.20 C ATOM 1192 NE ARGB2039 9.750 11.301 33.284 1.00 46.45 N ATOM 1193 CZ ARG B2039 9.59912.597 33.025 1.00 48.88 C ATOM 1194 NH1 ARG B2039 9.477 13.014 31.7701.00 48.84 N ATOM 1195 NH2 ARG B2039 9.570 13.478 34.018 1.00 49.51 NATOM 1196 C ARG B2039 7.926 8.585 36.397 1.00 27.40 C ATOM 1197 O ARGB2039 7.107 9.439 36.047 1.00 28.21 O ATOM 1198 N PHE B2040 7.717 7.28036.291 1.00 25.73 N ATOM 1199 CA PHE B2040 6.489 6.710 35.758 1.00 26.22C ATOM 1200 CB PHE B2040 6.546 5.185 35.916 1.00 24.31 C ATOM 1201 CGPHE B2040 5.265 4.477 35.573 1.00 26.63 C ATOM 1202 CD1 PHE B2040 4.8714.318 34.248 1.00 26.24 C ATOM 1203 CD2 PHE B2040 4.467 3.938 36.5791.00 26.94 C ATOM 1204 CE1 PHE B2040 3.698 3.627 33.930 1.00 27.58 CATOM 1205 CE2 PHE B2040 3.297 3.249 36.276 1.00 27.41 C ATOM 1206 CZ PHEB2040 2.911 3.090 34.950 1.00 27.69 C ATOM 1207 C PHE B2040 5.245 7.26236.463 1.00 26.33 C ATOM 1208 O PHE B2040 4.269 7.622 35.814 1.00 27.93O ATOM 1209 N THR B2041 5.287 7.324 37.792 1.00 27.19 N ATOM 1210 CA THRB2041 4.151 7.805 38.575 1.00 27.42 C ATOM 1211 CB THR B2041 4.328 7.48540.078 1.00 27.34 C ATOM 1212 OG1 THR B2041 5.504 8.132 40.577 1.0028.52 O ATOM 1213 CG2 THR B2041 4.458 5.986 40.294 1.00 28.04 C ATOM1214 C THR B2041 3.896 9.304 38.432 1.00 28.31 C ATOM 1215 O THR B20412.840 9.796 38.840 1.00 27.03 O ATOM 1216 N SER B2042 4.854 10.02437.853 1.00 28.11 N ATOM 1217 CA SER B2042 4.706 11.465 37.665 1.0031.34 C ATOM 1218 CB SER B2042 6.039 12.179 37.896 1.00 32.90 C ATOM1219 OG SER B2042 6.326 12.278 39.282 1.00 36.54 O ATOM 1220 C SER B20424.168 11.841 36.289 1.00 31.32 C ATOM 1221 O SER B2042 3.909 13.01236.018 1.00 30.89 O ATOM 1222 N LEU B2043 4.008 10.849 35.421 1.00 31.83N ATOM 1223 CA LEU B2043 3.487 11.088 34.077 1.00 31.92 C ATOM 1224 CBLEU B2043 4.293 10.300 33.038 1.00 29.48 C ATOM 1225 CG LEU B2043 5.78510.603 32.912 1.00 29.62 C ATOM 1226 CD1 LEU B2043 6.420 9.633 31.9211.00 29.54 C ATOM 1227 CD2 LEU B2043 5.985 12.035 32.462 1.00 29.33 CATOM 1228 C LEU B2043 2.039 10.623 34.058 1.00 33.01 C ATOM 1229 O LEUB2043 1.569 10.030 35.026 1.00 32.48 O ATOM 1230 N LYS B2044 1.33710.877 32.957 1.00 36.01 N ATOM 1231 CA LYS B2044 −0.060 10.469 32.8501.00 38.06 C ATOM 1232 CB LYS B2044 −0.967 11.586 33.375 1.00 39.86 CATOM 1233 CG LYS B2044 −2.402 11.149 33.619 1.00 43.44 C ATOM 1234 CDLYS B2044 −3.295 12.317 34.013 1.00 45.82 C ATOM 1235 CE LYS B2044−4.630 11.825 34.554 1.00 46.21 C ATOM 1236 NZ LYS B2044 −5.292 10.87933.615 1.00 47.83 N ATOM 1237 C LYS B2044 −0.472 10.116 31.422 1.0038.81 C ATOM 1238 O LYS B2044 0.225 10.438 30.459 1.00 39.23 O ATOM 1239N GLY B2045 −1.611 9.443 31.299 1.00 39.57 N ATOM 1240 CA GLY B2045−2.134 9.068 29.996 1.00 40.10 C ATOM 1241 C GLY B2045 −1.177 8.35529.062 1.00 40.74 C ATOM 1242 O GLY B2045 −0.513 7.394 29.454 1.00 41.23O ATOM 1243 N ARG B2046 −1.115 8.832 27.820 1.00 41.17 N ATOM 1244 CAARG B2046 −0.255 8.249 26.791 1.00 41.02 C ATOM 1245 CB ARG B2046 −0.3969.015 25.472 1.00 43.31 C ATOM 1246 CG ARG B2046 −1.812 9.081 24.9311.00 47.77 C ATOM 1247 CD ARG B2046 −1.882 9.873 23.627 1.00 50.51 CATOM 1248 NE ARG B2046 −3.260 10.180 23.244 1.00 52.23 N ATOM 1249 CZARG B2046 −3.611 10.768 22.103 1.00 52.56 C ATOM 1250 NH1 ARG B2046−4.890 11.012 21.844 1.00 52.50 N ATOM 1251 NH2 ARG B2046 −2.684 11.10721.217 1.00 53.75 N ATOM 1252 C ARG B2046 1.212 8.229 27.184 1.00 39.59C ATOM 1253 O ARG B2046 1.873 7.198 27.078 1.00 38.95 O ATOM 1254 N ARGB2047 1.718 9.375 27.631 1.00 38.59 N ATOM 1255 CA ARG B2047 3.117 9.49228.022 1.00 36.93 C ATOM 1256 CB ARG B2047 3.415 10.914 28.497 1.0039.53 C ATOM 1257 CG ARG B2047 3.284 11.965 27.408 1.00 43.89 C ATOM1258 CD ARG B2047 3.915 13.275 27.843 1.00 46.98 C ATOM 1259 NE ARGB2047 5.322 13.091 28.189 1.00 49.81 N ATOM 1260 CZ ARG B2047 6.14514.072 28.545 1.00 50.90 C ATOM 1261 NH1 ARG B2047 5.708 15.324 28.6031.00 51.65 N ATOM 1262 NH2 ARG B2047 7.409 13.800 28.845 1.00 52.13 NATOM 1263 C ARG B2047 3.543 8.496 29.095 1.00 34.22 C ATOM 1264 O ARGB2047 4.671 8.017 29.086 1.00 33.86 O ATOM 1265 N GLN B2048 2.646 8.18730.022 1.00 31.68 N ATOM 1266 CA GLN B2048 2.968 7.247 31.081 1.00 29.06C ATOM 1267 CB GLN B2048 1.844 7.212 32.121 1.00 29.98 C ATOM 1268 CGGLN B2048 2.236 6.524 33.420 1.00 32.80 C ATOM 1269 CD GLN B2048 1.0896.443 34.415 1.00 34.55 C ATOM 1270 OE1 GLN B2048 1.297 6.158 35.5961.00 36.97 O ATOM 1271 NE2 GLN B2048 −0.125 6.682 33.940 1.00 33.10 NATOM 1272 C GLN B2048 3.161 5.861 30.471 1.00 27.54 C ATOM 1273 O GLNB2048 4.134 5.170 30.769 1.00 26.96 O ATOM 1274 N ILE B2049 2.230 5.45929.612 1.00 25.61 N ATOM 1275 CA ILE B2049 2.318 4.159 28.961 1.00 24.60C ATOM 1276 CB ILE B2049 1.099 3.894 28.053 1.00 24.71 C ATOM 1277 CG2ILE B2049 1.310 2.606 27.254 1.00 25.39 C ATOM 1278 CG1 ILE B2049 −0.1743.814 28.906 1.00 25.99 C ATOM 1279 CD1 ILE B2049 −0.111 2.776 30.0041.00 26.01 C ATOM 1280 C ILE B2049 3.570 4.090 28.104 1.00 23.58 C ATOM1281 O ILE B2049 4.281 3.091 28.120 1.00 24.35 O ATOM 1282 N GLU B20503.828 5.160 27.360 1.00 22.52 N ATOM 1283 CA GLU B2050 4.985 5.23826.482 1.00 23.92 C ATOM 1284 CB GLU B2050 4.980 6.575 25.739 1.00 24.81C ATOM 1285 CG GLU B2050 6.216 6.842 24.901 1.00 27.69 C ATOM 1286 CDGLU B2050 6.470 5.767 23.859 1.00 30.29 C ATOM 1287 OE1 GLU B2050 5.5145.384 23.149 1.00 32.11 O ATOM 1288 OE2 GLU B2050 7.632 5.314 23.7401.00 29.75 O ATOM 1289 C GLU B2050 6.278 5.085 27.270 1.00 23.59 C ATOM1290 O GLU B2050 7.235 4.452 26.804 1.00 23.37 O ATOM 1291 N TYR B20516.304 5.666 28.466 1.00 23.27 N ATOM 1292 CA TYR B2051 7.487 5.58429.306 1.00 23.17 C ATOM 1293 CB TYR B2051 7.300 6.397 30.592 1.00 22.74C ATOM 1294 CG TYR B2051 8.520 6.367 31.492 1.00 22.74 C ATOM 1295 CD1TYR B2051 8.667 5.382 32.474 1.00 21.76 C ATOM 1296 CE1 TYR B2051 9.8185.317 33.263 1.00 23.29 C ATOM 1297 CD2 TYR B2051 9.555 7.288 31.3241.00 21.56 C ATOM 1298 CE2 TYR B2051 10.708 7.230 32.106 1.00 22.47 CATOM 1299 CZ TYR B2051 10.832 6.243 33.072 1.00 24.14 C ATOM 1300 OH TYRB2051 11.973 6.182 33.843 1.00 26.11 O ATOM 1301 C TYR B2051 7.749 4.12329.645 1.00 22.35 C ATOM 1302 O TYR B2051 8.834 3.603 29.397 1.00 21.78O ATOM 1303 N LEU B2052 6.735 3.470 30.200 1.00 21.05 N ATOM 1304 CA LEUB2052 6.820 2.069 30.581 1.00 20.91 C ATOM 1305 CB LEU B2052 5.486 1.62631.193 1.00 19.71 C ATOM 1306 CG LEU B2052 5.321 0.141 31.535 1.00 20.97C ATOM 1307 CD1 LEU B2052 6.463 −0.293 32.453 1.00 20.68 C ATOM 1308 CD2LEU B2052 3.953 −0.092 32.206 1.00 18.56 C ATOM 1309 C LEU B2052 7.1761.164 29.394 1.00 19.19 C ATOM 1310 O LEU B2052 8.055 0.305 29.502 1.0018.65 O ATOM 1311 N ALA B2053 6.501 1.365 28.264 1.00 18.96 N ATOM 1312CA ALA B2053 6.748 0.553 27.075 1.00 18.97 C ATOM 1313 CB ALA B20535.712 0.867 26.003 1.00 19.24 C ATOM 1314 C ALA B2053 8.153 0.777 26.5261.00 19.65 C ATOM 1315 O ALA B2053 8.811 −0.167 26.067 1.00 19.77 O ATOM1316 N GLY B2054 8.604 2.028 26.569 1.00 18.25 N ATOM 1317 CA GLY B20549.930 2.355 26.084 1.00 16.89 C ATOM 1318 C GLY B2054 11.004 1.74826.970 1.00 18.42 C ATOM 1319 O GLY B2054 12.072 1.344 26.488 1.00 17.94O ATOM 1320 N ARG B2055 10.731 1.692 28.270 1.00 16.40 N ATOM 1321 CAARG B2055 11.684 1.112 29.202 1.00 19.09 C ATOM 1322 CB ARG B2055 11.253−1.377 30.647 1.00 20.94 C ATOM 1323 CG ARG B2055 12.060 2.478 31.3291.00 20.89 C ATOM 1324 CD ARG B2055 11.968 3.790 30.570 1.00 24.51 CATOM 1325 NE ARG B2055 12.987 4.745 31.003 1.00 25.33 N ATOM 1326 CZ ARGB2055 13.239 5.897 30.388 1.00 25.95 C ATOM 1327 NH1 ARG B2055 12.5446.243 29.313 1.00 23.97 N ATOM 1328 NH2 ARG B2055 14.194 6.700 30.8431.00 25.82 N ATOM 1329 C ARG B2055 11.774 −0.386 28.932 1.00 18.98 CATOM 1330 O ARG B2055 12.855 −0.971 28.985 1.00 18.90 O ATOM 1331 N TRPB2056 10.632 −1.003 28.631 1.00 20.10 N ATOM 1332 CA TRP B2056 10.613−2.426 28.322 1.00 20.52 C ATOM 1333 CB TRP B2056 9.178 −2.930 28.1071.00 22.74 C ATOM 1334 CG TRP B2056 9.118 −4.394 27.738 1.00 26.17 CATOM 1335 CD2 TRP B2056 8.573 −5.459 28.527 1.00 27.99 C ATOM 1336 CE2TRP B2056 8.791 −6.661 27.815 1.00 28.39 C ATOM 1337 CE3 TRP B2056 7.924−5.516 29.767 1.00 27.60 C ATOM 1338 CD1 TRP B2056 9.623 −4.978 26.6071.00 26.87 C ATOM 1339 NE1 TRP B2056 9.432 −6.337 26.648 1.00 29.27 NATOM 1340 CZ2 TRP B2056 8.384 −7.906 28.301 1.00 29.62 C ATOM 1341 CZ3TRP B2056 7.516 −6.760 30.253 1.00 30.44 C ATOM 1342 CH2 TRP B2056 7.750−7.937 29.519 1.00 30.93 C ATOM 1343 C TRP B2056 11.430 −2.659 27.0561.00 18.69 C ATOM 1344 O TRP B2056 12.265 −3.562 27.007 1.00 15.35 OATOM 1345 N SER B2057 11.190 −1.843 26.032 1.00 18.10 N ATOM 1346 CA SERB2057 11.925 −1.993 24.778 1.00 19.73 C ATOM 1347 CB SER B2057 11.475−0.948 23.756 1.00 21.79 C ATOM 1348 OG SER B2057 10.174 −1.245 23.2731.00 30.44 O ATOM 1349 C SER B2057 13.427 −1.857 25.009 1.00 17.21 CATOM 1350 O SER B2057 14.207 −2.679 24.539 1.00 17.96 O ATOM 1351 N ALAB2058 13.821 −0.814 25.728 1.00 15.24 N ATOM 1352 CA ALA B2058 15.233−0.568 26.016 1.00 15.12 C ATOM 1353 CB ALA B2058 15.387 0.718 26.8191.00 14.34 C ATOM 1354 C ALA B2058 15.879 −1.724 26.768 1.00 15.45 CATOM 1355 O ALA B2058 16.981 −2.158 26.421 1.00 14.80 O ATOM 1356 N LYSB2059 15.203 −2.216 27.804 1.00 15.14 N ATOM 1357 CA LYS B2059 15.748−3.315 28.593 1.00 16.97 C ATOM 1358 CB LYS B2059 14.909 −3.523 29.8601.00 18.38 C ATOM 1359 CG LYS B2059 14.958 −2.303 30.796 1.00 17.80 CATOM 1360 CD LYS B2059 14.216 −2.546 32.097 1.00 19.77 C ATOM 1361 CELYS B2059 14.345 −1.327 33.021 1.00 19.57 C ATOM 1362 NZ LYS B205913.932 −1.624 34.417 1.00 20.44 N ATOM 1363 C LYS B2059 15.857 −4.60827.792 1.00 17.95 C ATOM 1364 O LYS B2059 16.805 −5.375 27.967 1.0016.15 O ATOM 1365 N GLU B2060 14.897 −4.844 26.904 1.00 17.88 N ATOM1366 CA GLU B2060 14.923 −6.041 26.070 1.00 17.87 C ATOM 1367 CB GLUB2060 13.551 −6.261 25.420 1.00 19.58 C ATOM 1368 CG GLU B2060 13.519−7.359 24.361 1.00 23.62 C ATOM 1369 CD GLU B2060 13.834 −8.753 24.8971.00 24.96 C ATOM 1370 OE1 GLU B2060 14.150 −8.906 26.099 1.00 27.91 OATOM 1371 OE2 GLU B2060 13.764 −9.707 24.096 1.00 27.02 O ATOM 1372 CGLU B2060 16.013 −5.885 24.999 1.00 17.82 C ATOM 1373 O GLU B2060 16.769−6.816 24.741 1.00 16.78 O ATOM 1374 N ALA B2061 16.106 −4.700 24.3961.00 15.53 N ATOM 1375 CA ALA B2061 17.126 −4.443 23.379 1.00 15.22 CATOM 1376 CB ALA B2061 17.017 −3.010 22.868 1.00 12.83 C ATOM 1377 C ALAB2061 18.514 −4.683 23.984 1.00 15.45 C ATOM 1378 O ALA B2061 19.396−5.252 23.337 1.00 15.13 O ATOM 1379 N PHE B2062 18.699 −4.248 25.2271.00 15.78 N ATOM 1380 CA PHE B2062 19.965 −4.441 25.923 1.00 16.16 CATOM 1381 CB PHE B2062 19.972 −3.664 27.244 1.00 18.34 C ATOM 1382 CGPHE B2062 21.173 −3.954 28.110 1.00 20.05 C ATOM 1383 CD1 PHE B206221.180 −5.055 28.972 1.00 20.65 C ATOM 1384 CD2 PHE B2062 22.311 −3.15828.030 1.00 20.37 C ATOM 1385 CE1 PHE B2062 22.304 −5.358 29.737 1.0020.45 C ATOM 1386 CE2 PHE B2062 23.450 −3.453 28.796 1.00 21.28 C ATOM1387 CZ PHE B2062 23.443 −4.552 29.647 1.00 20.21 C ATOM 1388 C PHEB2062 20.210 −5.930 26.195 1.00 17.69 C ATOM 1389 O PHE B2062 21.297−6.455 25.933 1.00 17.00 O ATOM 1390 N SER B2063 19.203 −6.608 26.7301.00 18.58 N ATOM 1391 CA SER B2063 19.336 −8.033 27.016 1.00 19.54 CATOM 1392 CB SER B2063 18.025 −8.584 27.565 1.00 19.74 C ATOM 1393 OGSER B2063 17.710 −7.950 28.793 1.00 22.28 O ATOM 1394 C SER B2063 19.733−8.789 25.753 1.00 20.63 C ATOM 1395 O SER B2063 20.574 −9.682 25.8031.00 18.71 O ATOM 1396 N LYS B2064 19.128 −8.430 24.620 1.00 19.41 NATOM 1397 CA LYS B2064 19.457 −9.088 23.362 1.00 20.24 C ATOM 1398 CBLYS B2064 18.447 −8.705 22.276 1.00 21.74 C ATOM 1399 CG LYS B206417.036 −9.246 22.553 1.00 21.35 C ATOM 1400 CD LYS B2064 16.007 −8.78521.525 1.00 21.53 C ATOM 1401 CE LYS B2064 16.378 −9.233 20.116 1.0019.60 C ATOM 1402 NZ LYS B2064 15.400 −8.764 19.091 1.00 19.68 N ATOM1403 C LYS B2064 20.875 −8.709 22.946 1.00 20.67 C ATOM 1404 O LYS B206421.573 −9.498 22.310 1.00 21.49 O ATOM 1405 N ALA B2065 21.303 −7.50223.308 1.00 17.85 N ATOM 1406 CA ALA B2065 22.660 −7.059 22.995 1.0019.57 C ATOM 1407 CB ALA B2065 22.826 −5.576 23.323 1.00 15.70 C ATOM1408 C ALA B2065 23.647 −7.892 23.820 1.00 20.80 C ATOM 1409 O ALA B206524.793 −8.096 23.414 1.00 18.12 O ATOM 1410 N MET B2066 23.199 −8.35924.985 1.00 22.49 N ATOM 1411 CA MET B2066 24.039 −9.187 25.849 1.0027.36 C ATOM 1412 CB MET B2066 23.608 −9.069 27.310 1.00 27.69 C ATOM1413 CG MET B2066 23.933 −7.749 27.971 1.00 30.93 C ATOM 1414 SD METB2066 25.678 −7.548 28.342 1.00 35.00 S ATOM 1415 CE MET B2066 25.840−8.691 29.727 1.00 35.63 C ATOM 1416 C MET B2066 23.927 −10.646 25.4161.00 28.77 C ATOM 1417 O MET B2066 24.570 −11.517 25.990 1.00 29.95 OATOM 1418 N GLY B2067 23.095 −10.906 24.411 1.00 30.61 N ATOM 1419 CAGLY B2067 22.927 −12.266 23.924 1.00 32.14 C ATOM 1420 C GLY B206721.816 −13.073 24.577 1.00 33.83 C ATOM 1421 O GLY B2067 21.728 −14.28224.353 1.00 35.17 O ATOM 1422 N THR B2068 20.964 −12.425 25.369 1.0033.49 N ATOM 1423 CA THR B2068 19.870 −13.124 26.048 1.00 35.61 C ATOM1424 CB THR B2068 20.225 −13.393 27.528 1.00 37.06 C ATOM 1425 OG1 THRB2068 20.480 −12.149 28.194 1.00 37.62 O ATOM 1426 CG2 THR B2068 21.461−14.274 27.622 1.00 40.72 C ATOM 1427 C THR B2068 18.519 −12.396 26.0081.00 34.51 C ATOM 1428 O THR B2068 18.212 −11.679 25.054 1.00 34.74 OATOM 1429 N GLY B2069 17.715 −12.598 27.051 1.00 34.71 N ATOM 1430 CAGLY B2069 16.403 −11.970 27.132 1.00 33.79 C ATOM 1431 C GLY B206916.195 −11.248 28.452 1.00 33.36 C ATOM 1432 O GLY B2069 16.823 −11.59029.455 1.00 32.35 O ATOM 1433 N ILE B2070 15.300 −10.263 28.467 1.0033.38 N ATOM 1434 CA ILE B2070 15.059 −9.487 29.680 1.00 34.29 C ATOM1435 CB ILE B2070 14.122 −8.283 29.401 1.00 33.36 C ATOM 1436 CG2 ILEB2070 12.761 −8.768 28.904 1.00 35.55 C ATOM 1437 CG1 ILE B2070 13.966−7.446 30.672 1.00 32.13 C ATOM 1438 CD1 ILE B2070 15.277 −6.991 31.2691.00 28.50 C ATOM 1439 C ILE B2070 14.514 −10.295 30.856 1.00 35.39 CATOM 1440 O ILE B2070 14.868 −10.039 32.008 1.00 35.52 O ATOM 1441 N SERB2071 13.666 −11.276 30.572 1.00 37.28 N ATOM 1442 CA SER B2071 13.104−12.104 31.630 1.00 39.77 C ATOM 1443 CB SER B2071 12.020 −13.025 31.0661.00 42.43 C ATOM 1444 OG SER B2071 11.433 −13.795 32.102 1.00 46.76 OATOM 1445 C SER B2071 14.189 −12.947 32.299 1.00 40.07 C ATOM 1446 O SERB2071 14.024 −13.402 33.428 1.00 39.81 O ATOM 1447 N LYS B2072 15.299−13.154 31.596 1.00 39.77 N ATOM 1448 CA LYS B2072 16.403 −13.940 32.1321.00 39.15 C ATOM 1449 CB LYS B2072 17.115 −14.689 31.007 1.00 40.68 CATOM 1450 CG LYS B2072 16.225 −15.656 30.252 1.00 43.38 C ATOM 1451 CDLYS B2072 16.996 −16.371 29.151 1.00 44.69 C ATOM 1452 CE LYS B207216.070 −17.260 28.342 1.00 46.81 C ATOM 1453 NZ LYS B2072 15.337 −18.22529.214 1.00 47.85 N ATOM 1454 C LYS B2072 17.396 −13.039 32.842 1.0038.30 C ATOM 1455 O LYS B2072 17.952 −13.401 33.879 1.00 38.50 O ATOM1456 N LEU B2073 17.613 −11.860 32.269 1.00 36.74 N ATOM 1457 CA LEUB2073 18.540 −10.883 32.821 1.00 34.89 C ATOM 1458 CB LEU B2073 18.817−9.803 31.766 1.00 35.18 C ATOM 1459 CG LEU B2073 20.010 −8.856 31.9101.00 35.71 C ATOM 1460 CD1 LEU B2073 19.804 −7.943 33.107 1.00 37.71 CATOM 1461 CD2 LEU B2073 21.296 −9.661 32.050 1.00 36.74 C ATOM 1462 CLEU B2073 17.961 −10.259 34.098 1.00 34.21 C ATOM 1463 O LEU B207318.683 −10.044 35.071 1.00 32.72 O ATOM 1464 N GLY B2074 16.658 −9.98234.090 1.00 33.08 N ATOM 1465 CA GLY B2074 16.014 −9.383 35.247 1.0032.12 C ATOM 1466 C GLY B2074 15.762 −7.897 35.053 1.00 30.96 C ATOM1467 O GLY B2074 16.702 −7.127 34.871 1.00 31.73 O ATOM 1468 N PHE B207514.497 −7.489 35.095 1.00 29.97 N ATOM 1469 CA PHE B2075 14.139 −6.08334.913 1.00 30.52 C ATOM 1470 CB PHE B2075 12.620 −5.896 34.973 1.0032.55 C ATOM 1471 CG PHE B2075 11.880 −6.511 33.822 1.00 33.89 C ATOM1472 CD1 PHE B2075 11.474 −7.843 33.868 1.00 35.06 C ATOM 1473 CD2 PHEB2075 11.578 −5.755 32.693 1.00 34.72 C ATOM 1474 CE1 PHE B2075 10.774−8.412 32.806 1.00 35.34 C ATOM 1475 CE2 PHE B2075 10.879 −6.316 31.6231.00 34.77 C ATOM 1476 CZ PHE B2075 10.477 −7.646 31.681 1.00 34.64 CATOM 1477 C PHE B2075 14.769 −5.146 35.934 1.00 29.45 C ATOM 1478 O PHEB2075 15.159 −4.025 35.599 1.00 30.37 O ATOM 1479 N GLN B2076 14.867−5.607 37.177 1.00 28.05 N ATOM 1480 CA GLN B2076 15.417 −4.796 38.2591.00 27.24 C ATOM 1481 CB GLN B2076 15.043 −5.420 39.607 1.00 27.56 CATOM 1482 CG GLN B2076 13.539 −5.436 39.859 1.00 27.74 C ATOM 1483 CDGLN B2076 12.929 −4.041 39.834 1.00 30.00 C ATOM 1484 OE1 GLN B207611.896 −3.807 39.193 1.00 31.13 O ATOM 1485 NE2 GLN B2076 13.563 −3.10740.536 1.00 28.51 N ATOM 1486 C GLN B2076 16.920 −4.538 38.198 1.0026.61 C ATOM 1487 O GLN B2076 17.430 −3.698 38.935 1.00 25.98 O ATOM1488 N ASP B2077 17.621 −5.251 37.320 1.00 26.64 N ATOM 1489 CA ASPB2077 19.062 −5.084 37.160 1.00 27.59 C ATOM 1490 CB ASP B2077 19.723−6.426 36.847 1.00 32.09 C ATOM 1491 CG ASP B2077 19.749 −7.352 38.0411.00 35.66 C ATOM 1492 OD1 ASP B2077 18.670 −7.841 38.440 1.00 39.93 OATOM 1493 OD2 ASP B2077 20.850 −7.584 38.586 1.00 40.87 O ATOM 1494 CASP B2077 19.403 −4.087 36.054 1.00 26.77 C ATOM 1495 O ASP B2077 20.571−3.825 35.779 1.00 25.66 O ATOM 1496 N LEU B2078 18.375 −3.539 35.4201.00 24.12 N ATOM 1497 CA LEU B2078 18.570 −2.571 34.356 1.00 23.25 CATOM 1498 CB LEU B2078 18.058 −3.118 33.018 1.00 23.97 C ATOM 1499 CGLEU B2078 18.750 −4.370 32.475 1.00 24.92 C ATOM 1500 CD1 LEU B207817.987 −4.914 31.276 1.00 23.04 C ATOM 1501 CD2 LEU B2078 20.180 −4.02132.089 1.00 26.74 C ATOM 1502 C LEU B2078 17.795 −1.321 34.702 1.0023.29 C ATOM 1503 O LEU B2078 16.669 −1.390 35.196 1.00 23.17 O ATOM1504 N GLU B2079 18.397 −0.173 34.446 1.00 21.42 N ATOM 1505 CA GLUB2079 17.724 1.075 34.716 1.00 21.45 C ATOM 1506 CB GLU B2079 18.1921.666 36.036 1.00 22.77 C ATOM 1507 CG GLU B2079 17.346 2.835 36.4771.00 24.03 C ATOM 1508 CD GLU B2079 17.726 3.340 37.848 1.00 25.73 CATOM 1509 OE1 GLU B2079 18.797 3.972 37.976 1.00 26.42 O ATOM 1510 OE2GLU B2079 16.950 3.099 38.798 1.00 27.63 O ATOM 1511 C GLU B2079 18.0142.055 33.600 1.00 20.55 C ATOM 1512 O GLU B2079 19.167 2.241 33.203 1.0020.96 O ATOM 1513 N VAL B2080 16.954 2.666 33.095 1.00 18.00 N ATOM 1514CA VAL B2080 17.055 3.648 32.033 1.00 18.55 C ATOM 1515 CB VAL B208016.268 3.211 30.769 1.00 16.14 C ATOM 1516 CG1 VAL B2080 16.429 4.26229.686 1.00 16.12 C ATOM 1517 CG2 VAL B2080 16.755 1.849 30.276 1.0014.67 C ATOM 1518 C VAL B2080 16.442 4.948 32.549 1.00 19.85 C ATOM 1519O VAL B2080 15.234 5.019 32.805 1.00 19.59 O ATOM 1520 N LEU B208117.279 5.966 32.708 1.00 20.39 N ATOM 1521 CA LEU B2081 16.825 7.27133.176 1.00 21.24 C ATOM 1522 CB LEU B2081 17.644 7.716 34.394 1.0021.31 C ATOM 1523 CG LEU B2081 17.683 6.758 35.593 1.00 22.71 C ATOM1524 CD1 LEU B2081 18.641 7.299 36.661 1.00 23.10 C ATOM 1525 CD2 LEUB2081 16.280 6.594 36.165 1.00 22.25 C ATOM 1526 C LEU B2081 17.0278.259 32.040 1.00 22.16 C ATOM 1527 O LEU B2081 17.421 7.882 30.934 1.0022.05 O ATOM 1528 N ASN B2082 16.755 9.526 32.309 1.00 22.54 N ATOM 1529CA ASN B2082 16.933 10.561 31.303 1.00 24.30 C ATOM 1530 CB ASN B208215.598 11.247 31.022 1.00 25.64 C ATOM 1531 CG ASN B2082 14.657 10.37130.207 1.00 27.22 C ATOM 1532 OD1 ASN B2082 14.779 10.280 28.982 1.0028.88 O ATOM 1533 ND2 ASN B2082 13.729 9.710 30.883 1.00 24.27 N ATOM1534 C ASN B2082 17.945 11.555 31.840 1.00 25.00 C ATOM 1535 O ASN B208217.860 11.958 33.001 1.00 23.46 O ATOM 1536 N ASN B2083 18.913 11.93931.010 1.00 25.22 N ATOM 1537 CA ASN B2083 19.920 12.890 31.454 1.0025.69 C ATOM 1538 CB ASN B2083 21.215 12.744 30.641 1.00 25.99 C ATOM1539 CG ASN B2083 21.013 12.961 29.153 1.00 27.46 C ATOM 1540 OD1 ASNB2083 20.173 13.758 28.729 1.00 25.62 O ATOM 1541 ND2 ASN B2083 21.81112.265 28.348 1.00 27.23 N ATOM 1542 C ASN B2083 19.410 14.330 31.3971.00 26.79 C ATOM 1543 O ASN B2083 18.216 14.571 31.215 1.00 25.77 OATOM 1544 N GLU B2084 20.322 15.281 31.559 1.00 29.60 N ATOM 1545 CA GLUB2084 19.982 16.701 31.563 1.00 31.78 C ATOM 1546 CB GLU B2084 21.23817.539 31.827 1.00 33.94 C ATOM 1547 CG GLU B2084 22.148 16.960 32.8961.00 39.23 C ATOM 1548 CD GLU B2084 22.774 15.640 32.470 1.00 41.35 CATOM 1549 OE1 GLU B2084 23.642 15.652 31.567 1.00 42.45 O ATOM 1550 OE2GLU B2084 22.390 −14.588 33.030 1.00 42.21 O ATOM 1551 C GLU B208419.351 17.153 30.253 1.00 30.81 C ATOM 1552 O GLU B2084 18.472 18.01330.242 1.00 29.26 O ATOM 1553 N ARG B2085 19.808 16.573 29.148 1.0030.86 N ATOM 1554 CA ARG B2085 19.291 16.940 27.838 1.00 31.05 C ATOM1555 CB ARG B2085 20.364 16.716 26.775 1.00 33.27 C ATOM 1556 CG ARGB2085 21.598 17.554 27.005 1.00 35.81 C ATOM 1557 CD ARG B2085 22.63617.335 25.928 1.00 38.24 C ATOM 1558 NE ARG B2085 23.735 18.286 26.0601.00 41.03 N ATOM 1559 CZ ARG B2085 24.544 18.349 27.110 1.00 42.41 CATOM 1560 NH1 ARG B2085 24.381 17.515 28.128 1.00 43.26 N ATOM 1561 NH2ARG B2085 25.523 19.239 27.138 1.00 44.30 N ATOM 1562 C ARG B2085 18.02416.190 27.465 1.00 30.14 C ATOM 1563 O ARG B2085 17.450 16.432 26.4081.00 31.11 O ATOM 1564 N GLY B2086 17.593 15.273 28.326 1.00 29.20 NATOM 1565 CA GLY B2086 16.371 14.530 28.057 1.00 27.93 C ATOM 1566 C GLYB2086 16.531 13.222 27.304 1.00 26.69 C ATOM 1567 O GLY B2086 15.54112.581 26.952 1.00 27.22 O ATOM 1568 N ALA B2087 17.770 12.818 27.0561.00 24.98 N ATOM 1569 CA ALA B2087 18.033 11.582 26.340 1.00 23.11 CATOM 1570 CB ALA B2087 19.358 11.692 25.589 1.00 24.73 C ATOM 1571 C ALAB2087 18.065 10.369 27.269 1.00 22.69 C ATOM 1572 O ALA B2087 18.61110.431 28.370 1.00 22.81 O ATOM 1573 N PRO B2088 17.481 9.242 26.8331.00 22.85 N ATOM 1574 CD PRO B2088 16.722 9.014 25.588 1.00 23.63 CATOM 1575 CA PRO B2088 17.485 8.039 27.674 1.00 21.17 C ATOM 1576 CB PROB2088 16.471 7.134 26.982 1.00 22.95 C ATOM 1577 CG PRO B2088 16.6507.489 25.528 1.00 24.16 C ATOM 1578 C PRO B2088 18.879 7.416 27.716 1.0020.46 C ATOM 1579 O PRO B2088 19.584 7.407 26.712 1.00 18.12 O ATOM 1580N TYR B2089 19.280 6.906 28.878 1.00 19.76 N ATOM 1581 CA TYR B208920.593 6.275 29.019 1.00 19.97 C ATOM 1582 CB TYR B2089 21.660 7.33729.324 1.00 20.30 C ATOM 1583 CG TYR B2089 21.605 7.850 30.743 1.0021.25 C ATOM 1584 CD1 TYR B2089 22.471 7.347 31.719 1.00 23.06 C ATOM1585 CE1 TYR B2089 22.386 7.765 33.046 1.00 22.62 C ATOM 1586 CD2 TYRB2089 20.651 8.793 31.128 1.00 21.67 C ATOM 1587 CE2 TYR B2089 20.5579.218 32.454 1.00 23.51 C ATOM 1588 CZ TYR B2089 21.429 8.693 33.4041.00 22.23 C ATOM 1589 OH TYR B2089 21.327 9.078 34.715 1.00 23.91 OATOM 1590 C TYR B2089 20.547 5.246 30.148 1.00 18.84 C ATOM 1591 O TYRB2089 19.738 5.356 31.066 1.00 16.92 O ATOM 1592 N PHE B2090 21.4084.237 30.076 1.00 19.96 N ATOM 1593 CA PHE B2090 21.432 3.218 31.1161.00 20.18 C ATOM 1594 CB PHE B2090 22.015 1.906 30.588 1.00 18.86 CATOM 1595 CG PHE B2090 21.031 1.078 29.813 1.00 17.77 C ATOM 1596 CD1PHE B2090 20.843 1.282 28.452 1.00 18.34 C ATOM 1597 CD2 PHE B209020.276 0.102 30.455 1.00 17.66 C ATOM 1598 CE1 PHE B2090 19.915 0.52327.737 1.00 16.58 C ATOM 1599 CE2 PHE B2090 19.344 −0.666 29.751 1.0016.83 C ATOM 1600 CZ PHE B2090 19.166 −0.453 28.393 1.00 18.42 C ATOM1601 C PHE B2090 22.249 3.683 32.307 1.00 21.96 C ATOM 1602 O PHE B209023.464 3.837 32.215 1.00 21.17 O ATOM 1603 N SER B2091 21.569 3.91633.423 1.00 21.79 N ATOM 1604 CA SER B2091 22.233 4.346 34.642 1.0023.26 C ATOM 1605 CB SER B2091 21.269 5.171 35.498 1.00 24.51 C ATOM1606 OG SER B2091 20.046 4.473 35.689 1.00 27.15 O ATOM 1607 C SER B209122.676 −3.101 35.406 1.00 24.05 C ATOM 1608 O SER B2091 23.572 3.15836.241 1.00 22.27 O ATOM 1609 N GLN B2092 22.039 1.974 35.100 1.00 24.23N ATOM 1610 CA GLN B2092 22.343 0.702 35.750 1.00 26.68 C ATOM 1611 CBGLN B2092 21.324 0.420 36.858 1.00 30.19 C ATOM 1612 CG GLN B2092 21.7380.888 38.236 1.00 36.96 C ATOM 1613 CD GLN B2092 22.791 −0.013 38.8461.00 41.69 C ATOM 1614 OE1 GLN B2092 23.923 −0.086 38.360 1.00 44.08 OATOM 1615 NE2 GLN B2092 22.419 −0.719 39.914 1.00 43.86 N ATOM 1616 CGLN B2092 22.318 −0.450 34.755 1.00 25.68 C ATOM 1617 O GLN B2092 21.350−0.628 34.015 1.00 25.64 O ATOM 1618 N ALA B2093 23.378 −1.243 34.7501.00 24.06 N ATOM 1619 CA ALA B2093 23.451 −2.379 33.845 1.00 24.55 CATOM 1620 CB ALA B2093 23.544 −1.896 32.401 1.00 23.95 C ATOM 1621 C ALAB2093 24.654 −3.240 34.182 1.00 24.42 C ATOM 1622 O ALA B2093 25.669−2.737 34.662 1.00 23.73 O ATOM 1623 N PRO B2094 24.542 −4.560 33.9581.00 24.28 N ATOM 1624 CD PRO B2094 23.286 −5.266 33.634 1.00 24.45 CATOM 1625 CA PRO B2094 25.625 −5.509 34.226 1.00 24.13 C ATOM 1626 CBPRO B2094 24.882 −6.827 34.404 1.00 24.53 C ATOM 1627 CG PRO B209423.752 −6.693 33.412 1.00 25.43 C ATOM 1628 C PRO B2094 26.575 −5.53233.033 1.00 25.18 C ATOM 1629 O PRO B2094 26.687 −6.538 32.330 1.0027.39 O ATOM 1630 N PHE B2095 27.237 −4.406 32.795 1.00 25.59 N ATOM1631 CA PHE B2095 28.166 −4.276 31.674 1.00 26.28 C ATOM 1632 CB PHEB2095 27.394 −3.937 30.392 1.00 26.01 C ATOM 1633 CG PHE B2095 28.264−3.808 29.176 1.00 25.16 C ATOM 1634 CD1 PHE B2095 28.289 −2.622 28.4481.00 23.33 C ATOM 1635 CD2 PHE B2095 29.070 −4.864 28.766 1.00 24.13 CATOM 1636 CE1 PHE B2095 29.106 −2.488 27.333 1.00 23.09 C ATOM 1637 CE2PHE B2095 29.890 −4.739 27.652 1.00 24.48 C ATOM 1638 CZ PHE B209529.906 −3.542 26.933 1.00 21.85 C ATOM 1639 C PHE B2095 29.157 −3.16832.000 1.00 25.62 C ATOM 1640 O PHE B2095 28.768 −2.080 32.413 1.0026.70 O ATOM 1641 N SER B2096 30.438 −3.441 .31.804 1.00 26.81 N ATOM1642 CA SER B2096 31.472 −2.466 32.122 1.00 27.94 C ATOM 1643 CB SERB2096 32.750 −3.203 32.531 1.00 27.66 C ATOM 1644 OG SER B2096 33.144−4.111 31.518 1.00 29.62 O ATOM 1645 C SER B2096 31.787 −1.469 31.0071.00 27.71 C ATOM 1646 O SER B2096 32.430 −0.452 31.249 1.00 27.75 OATOM 1647 N GLY B2097 31.325 −1.746 29.792 1.00 26.55 N ATOM 1648 CA GLYB2097 31.611 −0.847 28.690 1.00 23.99 C ATOM 1649 C GLY B2097 30.6110.274 28.499 1.00 23.68 C ATOM 1650 O GLY B2097 29.869 0.639 29.413 1.0022.73 O ATOM 1651 N LYS B2098 30.606 0.838 27.299 1.00 23.32 N ATOM 1652CA LYS B2098 29.682 1.912 26.975 1.00 23.52 C ATOM 1653 CB LYS B209830.323 2.896 25.995 1.00 25.66 C ATOM 1654 CG LYS B2098 31.546 3.59926.562 1.00 29.30 C ATOM 1655 CD LYS B2098 32.162 4.532 25.545 1.0031.81 C ATOM 1656 CE LYS B2098 33.364 5.247 26.128 1.00 35.72 C ATOM1657 NZ LYS B2098 33.970 6.194 25.154 1.00 38.45 N ATOM 1658 C LYS B209828.438 1.302 26.356 1.00 21.94 C ATOM 1659 O LYS B2098 28.518 0.35025.570 1.00 20.64 O ATOM 1660 N ILE B2099 27.294 1.862 26.721 1.00 20.44N ATOM 1661 CA ILE B2099 26.008 1.400 26.236 1.00 19.38 C ATOM 1662 CBILE B2099 25.109 1.012 27.421 1.00 19.92 C ATOM 1663 CG2 ILE B209923.804 0.423 26.919 1.00 20.26 C ATOM 1664 CG1 ILE B2099 25.839 −0.00828.302 1.00 19.45 C ATOM 1665 CD1 ILE B2099 25.193 −0.230 29.663 1.0021.98 C ATOM 1666 C ILE B2099 25.352 2.529 25.444 1.00 19.88 C ATOM 1667O ILE B2099 24.950 3.546 26.011 1.00 19.12 O ATOM 1668 N TRP B210025.267 2.352 24.129 1.00 19.02 N ATOM 1669 CA TRP B2100 24.662 3.35123.265 1.00 17.64 C ATOM 1670 CB TRP B2100 25.430 3.431 21.951 1.0019.81 C ATOM 1671 CG TRP B2100 26.840 3.861 22.165 1.00 20.97 C ATOM1672 CD2 TRP B2100 27.295 5.202 22.383 1.00 21.20 C ATOM 1673 CE2 TRPB2100 28.680 5.137 22.640 1.00 20.87 C ATOM 1674 CE3 TRP B2100 26.6616.454 22.393 1.00 22.40 C ATOM 1675 CD1 TRP B2100 27.938 3.059 22.2891.00 22.80 C ATOM 1676 NE1 TRP B2100 29.050 3.818 22.576 1.00 21.53 NATOM 1677 CZ2 TRP B2100 29.448 6.279 22.901 1.00 21.01 C ATOM 1678 CZ3TRP B2100 27.425 7.591 22.654 1.00 19.76 C ATOM 1679 CH2 TRP B210028.803 7.492 22.905 1.00 20.24 C ATOM 1680 C TRP B2100 23.207 2.98723.023 1.00 17.98 C ATOM 1681 O TRP B2100 22.889 2.033 22.308 1.00 19.71O ATOM 1682 N LEU B2101 22.323 3.761 23.632 1.00 16.57 N ATOM 1683 CALEU B2101 20.897 3.527 23.524 1.00 15.94 C ATOM 1684 CB LEU B2101 20.2923.364 24.925 1.00 14.34 C ATOM 1685 CG LEU B2101 18.756 3.387 25.0131.00 15.83 C ATOM 1686 CD1 LEU B2101 18.195 2.073 24.455 1.00 11.99 CATOM 1687 CD2 LEU B2101 18.324 3.555 26.467 1.00 14.03 C ATOM 1688 C LEUB2101 20.142 4.632 22.810 1.00 16.46 C ATOM 1689 O LEU B2101 20.4645.807 22.937 1.00 14.73 O ATOM 1690 N SER B2102 19.133 4.232 22.047 1.0017.13 N ATOM 1691 CA SER B2102 18.260 5.182 21.380 1.00 16.87 C ATOM1692 CB SER B2102 18.683 5.449 19.945 1.00 17.85 C ATOM 1693 OG SERB2102 17.856 6.473 19.405 1.00 18.12 O ATOM 1694 C SER B2102 16.8664.577 21.393 1.00 15.72 C ATOM 1695 O SER B2102 16.706 3.368 21.230 1.0014.46 O ATOM 1696 N ILE B2103 15.863 5.414 21.613 1.00 15.13 N ATOM 1697CA ILE B2103 14.478 4.948 21.646 1.00 17.16 C ATOM 1698 CB ILE B210313.897 5.031 23.070 1.00 17.86 C ATOM 1699 CG2 ILE B2103 12.439 4.56023.063 1.00 17.77 C ATOM 1700 CG1 ILE B2103 14.765 4.215 24.036 1.0018.09 C ATOM 1701 CD1 ILE B2103 14.406 4.396 25.497 1.00 17.05 C ATOM1702 C ILE B2103 13.645 5.852 20.749 1.00 17.44 C ATOM 1703 O ILE B210313.886 7.055 20.684 1.00 17.70 O ATOM 1704 N SER B2104 12.675 5.27520.053 1.00 17.76 N ATOM 1705 CA SER B2104 11.803 6.065 19.187 1.0019.81 C ATOM 1706 CB SER B2104 12.355 6.117 17.759 1.00 19.27 C ATOM1707 OG SER B2104 11.570 6.964 16.930 1.00 20.56 O ATOM 1708 C SER B210410.426 5.432 19.189 1.00 20.64 C ATOM 1709 O SER B2104 10.290 4.21319.338 1.00 22.59 O ATOM 1710 N HIS B2105 9.396 6.246 19.020 1.00 20.13N ATOM 1711 CA HIS B2105 8.055 5.698 19.028 1.00 22.93 C ATOM 1712 CBHIS B2105 7.456 5.812 20.432 1.00 23.19 C ATOM 1713 CG HIS B2105 7.2777.227 20.890 1.00 24.84 C ATOM 1714 CD2 HIS B2105 6.221 8.069 20.7851.00 26.28 C ATOM 1715 ND1 HIS B2105 8.284 7.950 21.490 1.00 26.53 NATOM 1716 CE1 HIS B2105 7.858 9.176 21.737 1.00 25.54 C ATOM 1717 NE2HIS B2105 6.609 9.275 21.318 1.00 26.28 N ATOM 1718 C HIS B2105 7.1166.375 18.050 1.00 21.93 C ATOM 1719 O HIS B2105 7.395 7.460 17.554 1.0021.72 O ATOM 1720 N THR B2106 6.016 5.687 17.769 1.00 23.48 N ATOM 1721CA THR B2106 4.941 6.183 16.919 1.00 25.16 C ATOM 1722 CB THR B21064.605 5.242 15.755 1.00 25.21 C ATOM 1723 OG1 THR B2106 4.222 3.96516.278 1.00 25.03 O ATOM 1724 CG2 THR B2106 5.791 5.089 14.823 1.0025.52 C ATOM 1725 C THR B2106 3.775 6.121 17.894 1.00 25.80 C ATOM 1726O THR B2106 3.978 5.862 19.081 1.00 24.98 O ATOM 1727 N ASP B2107 2.5596.329 17.406 1.00 25.90 N ATOM 1728 CA ASP B2107 1.397 6.284 18.285 1.0027.49 C ATOM 1729 CB ASP B2107 0.169 6.862 17.574 0.05 26.86 C ATOM 1730CG ASP B2107 0.127 8.380 17.621 0.05 26.92 C ATOM 1731 OD1 ASP B21071.090 9.023 17.157 0.05 27.01 O ATOM 1732 OD2 ASP B2107 −0.874 8.93018.125 0.05 26.97 O ATOM 1733 C ASP B2107 1.085 4.877 18.788 1.00 27.36C ATOM 1734 O ASP B2107 0.493 4.717 19.854 1.00 29.78 O ATOM 1735 N GLNB2108 1.482 3.858 18.032 1.00 25.07 N ATOM 1736 CA GLN B2108 1.207 2.48318.433 1.00 25.09 C ATOM 1737 CB GLN B2108 0.523 1.736 17.293 1.00 26.05C ATOM 1738 CG GLN B2108 −0.728 2.395 16.780 1.00 29.37 C ATOM 1739 CDGLN B2108 −1.145 1.827 15.445 1.00 31.53 C ATOM 1740 OE1 GLN B2108−0.362 1.822 14.492 1.00 31.44 O ATOM 1741 NE2 GLN B2108 −2.379 1.34515.363 1.00 31.86 N ATOM 1742 C GLN B2108 2.412 1.658 18.876 1.00 24.58C ATOM 1743 O GLN B2108 2.251 0.710 19.650 1.00 22.64 O ATOM 1744 N PHEB2109 3.606 2.000 18.386 1.00 23.20 N ATOM 1745 CA PHE B2109 4.800 1.22918.725 1.00 22.81 C ATOM 1746 CB PHE B2109 5.309 0.456 17.501 1.00 24.68C ATOM 1747 CG PHE B2109 4.236 −0.250 16.721 1.00 26.08 C ATOM 1748 CD1PHE B2109 3.701 0.329 15.576 1.00 26.47 C ATOM 1749 CD2 PHE B2109 3.783−1.505 17.110 1.00 27.02 C ATOM 1750 CE1 PHE B2109 2.729 −0.336 14.8251.00 28.36 C ATOM 1751 CE2 PHE B2109 2.810 −2.177 16.366 1.00 27.54 CATOM 1752 CZ PHE B2109 2.287 −1.592 15.224 1.00 28.20 C ATOM 1753 C PHEB2109 5.980 2.037 19.260 1.00 21.56 C ATOM 1754 O PHE B2109 6.096 3.23319.027 1.00 22.22 O ATOM 1755 N VAL B2110 6.872 1.358 19.969 1.00 21.04N ATOM 1756 CA VAL B2110 8.073 2.005 20.485 1.00 20.21 C ATOM 1757 CBVAL B2110 7.982 2.279 22.006 1.00 19.74 C ATOM 1758 CG1 VAL B2110 7.6491.001 22.751 1.00 21.12 C ATOM 1759 CG2 VAL B2110 9.307 2.861 22.5041.00 21.25 C ATOM 1760 C VAL B2110 9.230 1.063 20.197 1.00 20.24 C ATOM1761 O VAL B2110 9.160 −0.128 20.523 1.00 21.27 O ATOM 1762 N THR B211110.276 1.580 19.557 1.00 19.29 N ATOM 1763 CA THR B2111 11.440 0.76319.235 1.00 20.44 C ATOM 1764 CB THR B2111 11.759 0.788 17.725 1.0022.75 C ATOM 1765 OG1 THR B2111 12.116 2.120 17.337 1.00 27.12 O ATOM1766 CG2 THR B2111 10.550 0.353 16.911 1.00 26.61 C ATOM 1767 C THRB2111 12.668 1.270 19.982 1.00 19.21 C ATOM 1768 O THR B2111 12.7802.455 20.278 1.00 18.06 O ATOM 1769 N ALA B2112 13.581 0.353 20.280 1.0018.16 N ATOM 1770 CA ALA B2112 14.810 0.675 20.988 1.00 17.59 C ATOM1771 CB ALA B2112 14.715 0.231 22.442 1.00 14.54 C ATOM 1772 C ALA B211215.951 −0.052 20.292 1.00 17.15 C ATOM 1773 O ALA B2112 15.776 −1.16319.788 1.00 15.26 O ATOM 1774 N SER B2113 17.111 0.588 20.258 1.00 16.75N ATOM 1775 CA SER B2113 18.297 0.015 19.631 1.00 17.12 C ATOM 1776 CBSER B2113 18.574 0.705 18.287 1.00 17.55 C ATOM 1777 OG SER B2113 19.6740.112 17.603 1.00 19.24 O ATOM 1778 C SER B2113 19.470 0.227 20.588 1.0016.82 C ATOM 1779 O SER B2113 19.677 1.327 21.092 1.00 17.25 O ATOM 1780N VAL B2114 20.220 −0.837 20.840 1.00 16.23 N ATOM 1781 CA VAL B211421.364 −0.778 21.736 1.00 15.71 C ATOM 1782 CB VAL B2114 21.129 −1.59123.017 1.00 13.94 C ATOM 1783 CG1 VAL B2114 22.451 −1.731 23.784 1.0014.11 C ATOM 1784 CG2 VAL B2114 20.070 −0.923 23.877 1.00 10.51 C ATOM1785 C VAL B2114 22.617 −1.345 21.106 1.00 16.39 C ATOM 1786 O VAL B211422.578 −2.412 20.492 1.00 16.76 O ATOM 1787 N ILE B2115 23.724 −0.62521.259 1.00 14.68 N ATOM 1788 CA ILE B2115 25.014 −1.093 20.763 1.0015.53 C ATOM 1789 CB ILE B2115 25.589 −0.191 19.664 1.00 16.82 C ATOM1790 CG2 ILE B2115 26.983 −0.702 19.253 1.00 14.25 C ATOM 1791 CG1 ILEB2115 24.649 −0.168 18.461 1.00 17.22 C ATOM 1792 CD1 ILE B2115 25.0200.874 17.423 1.00 18.67 C ATOM 1793 C ILE B2115 25.956 −1.039 21.9561.00 16.88 C ATOM 1794 O ILE B2115 26.080 0.006 22.614 1.00 16.02 O ATOM1795 N LEU B2116 26.603 −2.164 22.237 1.00 14.98 N ATOM 1796 CA LEUB2116 27.529 −2.259 23.361 1.00 16.57 C ATOM 1797 CB LEU B2116 27.365−3.605 24.067 1.00 16.24 C ATOM 1798 CG LEU B2116 25.945 −3.870 24.5781.00 16.49 C ATOM 1799 CD1 LEU B2116 25.872 −5.256 25.197 1.00 15.73 CATOM 1800 CD2 LEU B2116 25.563 −2.803 25.591 1.00 15.00 C ATOM 1801 CLEU B2116 28.945 −2.121 22.852 1.00 17.64 C ATOM 1802 O LEU B2116 29.297−2.703 21.827 1.00 17.88 O ATOM 1803 N GLU B2117 29.763 −1.373 23.5841.00 19.16 N ATOM 1804 CA GLU B2117 31.132 −1.136 23.166 1.00 22.44 CATOM 1805 CB GLU B2117 31.199 0.229 22.473 1.00 21.55 C ATOM 1806 CG GLUB2117 32.570 0.672 22.003 1.00 26.09 C ATOM 1807 CD GLU B2117 32.5632.110 21.477 1.00 26.21 C ATOM 1808 OE1 GLU B2117 31.958 2.997 22.1321.00 24.17 O ATOM 1809 OE2 GLU B2117 33.170 2.355 20.412 1.00 27.59 OATOM 1810 C GLU B2117 32.116 −1.191 24.335 1.00 24.52 C ATOM 1811 O GLUB2117 31.829 −0.711 25.432 1.00 21.96 O ATOM 1812 N GLU B2118 33.266−1.806 24.084 1.00 26.38 N ATOM 1813 CA GLU B2118 34.331 −1.920 25.0701.00 31.02 C ATOM 1814 CB GLU B2118 34.781 −3.373 25.209 1.00 33.06 CATOM 1815 CG GLU B2118 33.888 −4.220 26.082 1.00 38.01 C ATOM 1816 CDGLU B2118 34.094 −3.939 27.552 1.00 42.42 C ATOM 1817 OE1 GLU B211833.776 −2.816 27.998 1.00 44.59 O ATOM 1818 OE2 GLU B2118 34.584 −4.84528.262 1.00 45.87 O ATOM 1819 C GLU B2118 35.482 −1.091 24.533 1.0032.66 C ATOM 1820 O GLU B2118 35.880 −0.108 25.197 1.00 35.23 O ATOM1821 OXT GLU B2118 35.958 −1.442 23.431 1.00 32.94 O TER 1822 GLU B2118ATOM 1823 CB MET C3003 37.039 0.395 12.081 1.00 32.22 C ATOM 1824 CG METC3003 37.297 −0.447 10.845 1.00 36.68 C ATOM 1825 SD MET C3003 38.4830.306 9.716 1.00 46.15 S ATOM 1826 CE MET C3003 37.454 1.490 8.876 1.0042.14 C ATOM 1827 C MET C3003 34.864 −0.764 12.331 1.00 25.86 C ATOM1828 O MET C3003 34.821 −1.903 11.864 1.00 26.11 O ATOM 1829 N MET C300336.772 −1.388 13.778 1.00 27.93 N ATOM 1830 CA MET C3003 36.090 −0.26413.082 1.00 27.91 C ATOM 1831 N ILE C3004 33.866 0.097 12.219 1.00 23.54N ATOM 1832 CA ILE C3004 32.655 −0.247 11.500 1.00 21.79 C ATOM 1833 CBILE C3004 31.503 0.697 11.890 1.00 22.07 C ATOM 1834 CG2 ILE C300430.259 0.377 11.063 1.00 20.08 C ATOM 1835 CG1 ILE C3004 31.212 0.56013.391 1.00 21.69 C ATOM 1836 CD1 ILE C3004 30.181 1530 13.913 1.0020.52 C ATOM 1837 C ILE C3004 32.942 −0.109 10.005 1.00 22.42 C ATOM1838 O ILE C3004 33.595 0.843 9.578 1.00 21.61 O ATOM 1839 N VAL C300532.483 −1.071 9.212 1.00 21.57 N ATOM 1840 CA VAL C3005 32.692 −0.9997.777 1.00 22.56 C ATOM 1841 CB VAL C3005 33.600 −2.145 7.265 1.00 24.27C ATOM 1842 CG1 VAL C3005 34.954 −2.087 7.975 1.00 23.54 C ATOM 1843 CG2VAL C3005 32.924 −3.487 7.478 1.00 25.12 C ATOM 1844 C VAL C3005 31.349−1.036 7.049 1.00 22.07 C ATOM 1845 O VAL C3005 31.297 −0.988 5.823 1.0022.90 O ATOM 1846 N GLY C3006 30.264 −1.106 7.814 1.00 19.77 N ATOM 1847CA GLY C3006 28.946 −1.124 7.207 1.00 18.90 C ATOM 1848 C GLY C300627.840 −1.111 8.240 1.00 18.66 C ATOM 1849 O GLY C3006 28.039 −1.5429.375 1.00 19.40 O ATOM 1850 N HIS C3007 26.679 −0.595 7.849 1.00 17.60N ATOM 1851 CA HIS C3007 25.517 −0.544 8.726 1.00 17.25 C ATOM 1852 CBHIS C3007 25.541 0.709 9.615 1.00 17.61 C ATOM 1853 CG HIS C3007 24.3150.867 10.469 1.00 17.57 C ATOM 1854 CD2 HIS C3007 23.615 1.967 10.8341.00 17.24 C ATOM 1855 ND1 HIS C3007 23.686 −0.203 11.072 1.00 17.16 NATOM 1856 CE1 HIS C3007 22.651 0.231 11.771 1.00 17.81 C ATOM 1857 NE2HIS C3007 22.585 1.545 11.644 1.00 18.60 N ATOM 1858 C HIS C3007 24.264−0.540 7.867 1.00 17.20 C ATOM 1859 O HIS C3007 24.138 0.249 6.924 1.0017.44 O ATOM 1860 N GLY C3008 23.335 −1.427 8.187 1.00 16.34 N ATOM 1861CA GLY C3008 22.111 −1.484 7.416 1.00 18.39 C ATOM 1862 C GLY C300820.925 −1.924 8.242 1.00 19.04 C ATOM 1863 O GLY C3008 21.060 −2.7529.145 1.00 19.03 O ATOM 1864 N ILE C3009 19.761 −1.352 7.944 1.00 18.83N ATOM 1865 CA ILE C3009 18.542 −1.718 8.640 1.00 19.42 C ATOM 1866 CBILE C3009 18.047 −0.598 9.594 1.00 18.51 C ATOM 1867 CG2 ILE C300919.197 −0.150 10.493 1.00 20.36 C ATOM 1868 CG1 ILE C3009 17.505 0.5858.797 1.00 17.23 C ATOM 1869 CD1 ILE C3009 16.778 1.592 9.643 1.00 13.66C ATOM 1870 C ILE C3009 17.473 −1.992 7.602 1.00 18.70 C ATOM 1871 O ILEC3009 17.647 −1.685 6.427 1.00 15.95 O ATOM 1872 N ASP C3010 16.369−2.585 8.037 1.00 19.75 N ATOM 1873 CA ASP C3010 15.278 −2.882 7.1291.00 20.22 C ATOM 1874 CB ASP C3010 15.550 −4.184 6.358 1.00 20.94 CATOM 1875 CG ASP C3010 14.474 −4.487 5.310 1.00 22.14 C ATOM 1876 OD1ASP C3010 14.480 −3.844 4.236 1.00 22.44 O ATOM 1877 OD2 ASP C301013.617 −5.363 5.561 1.00 20.92 O ATOM 1878 C ASP C3010 14.007 −3.0477.932 1.00 21.28 C ATOM 1879 O ASP C3010 14.042 −3.500 9.078 1.00 21.26O ATOM 1880 N ILE C3011 12.893 −2.646 7.333 1.00 19.66 N ATOM 1881 CAILE C3011 11.588 −2.813 7.949 1.00 20.09 C ATOM 1882 CB ILE C3011 10.959−1.476 8.400 1.00 20.39 C ATOM 1883 CG2 ILE C3011 10.910 −0.478 7.2341.00 16.27 C ATOM 1884 CG1 ILE C3011 9.561 −1.753 8.971 1.00 20.84 CATOM 1885 CD1 ILE C3011 9.081 −0.712 9.969 1.00 21.63 C ATOM 1886 C ILEC3011 10.777 −3.440 6.825 1.00 21.21 C ATOM 1887 O ILE C3011 10.866−3.006 5.678 1.00 21.49 O ATOM 1888 N GLU C3012 10.018 −4.481 7.140 1.0021.79 N ATOM 1889 CA GLU C3012 9.249 −5.174 6.120 1.00 23.44 C ATOM 1890CB GLU C3012 10.024 −6.415 5.656 1.00 24.63 C ATOM 1891 CG GLU C30129.269 −7.309 4.667 1.00 27.74 C ATOM 1892 CD GLU C3012 9.351 −6.8123.237 1.00 27.70 C ATOM 1893 OE1 GLU C3012 9.663 −5.626 3.032 1.00 28.89O ATOM 1894 OE2 GLU C3012 9.091 −7.612 2.314 1.00 31.17 O ATOM 1895 CGLU C3012 7.873 −5.583 6.625 1.00 23.57 C ATOM 1896 O GLU C3012 7.750−6.258 7.647 1.00 22.12 O ATOM 1897 N GLU C3013 6.840 −5.170 5.904 1.0023.45 N ATOM 1898 CA GLU C3013 5.491 −5.519 6.286 1.00 24.76 C ATOM 1899CB GLU C3013 4.479 −4.613 5.571 1.00 29.22 C ATOM 1900 CG GLU C30133.662 −3.731 6.531 1.00 33.17 C ATOM 1901 CD GLU C3013 3.915 −2.2426.349 1.00 38.85 C ATOM 1902 OE1 GLU C3013 3.660 −1.719 5.238 1.00 44.44O ATOM 1903 OE2 GLU C3013 4.359 −1.586 7.318 1.00 38.04 O ATOM 1904 CGLU C3013 5.238 −6.993 5.963 1.00 24.30 C ATOM 1905 O GLU C3013 5.643−7.502 4.910 1.00 21.31 O ATOM 1906 N LEU C3014 4.599 −7.685 6.898 1.0022.97 N ATOM 1907 CA LEU C3014 4.287 −9.092 6.712 1.00 26.19 C ATOM 1908CB LEU C3014 3.531 −9.613 7.939 1.00 28.12 C ATOM 1909 CG LEU C30144.251 −10.630 8.829 1.00 31.98 C ATOM 1910 CD1 LEU C3014 5.647 −10.1449.191 1.00 31.03 C ATOM 1911 CD2 LEU C3014 3.414 −10.868 10.083 1.0033.69 C ATOM 1912 C LEU C3014 3.453 −9.308 5.439 1.00 25.44 C ATOM 1913O LEU C3014 3.554 −10.345 4.793 1.00 25.78 O ATOM 1914 N ALA C3015 2.644−8.320 5.073 1.00 24.83 N ATOM 1915 CA ALA C3015 1.801 −8.438 3.879 1.0027.12 C ATOM 1916 CB ALA C3015 0.915 −7.206 3.747 1.00 27.24 C ATOM 1917C ALA C3015 2.592 −8.659 2.584 1.00 27.01 C ATOM 1918 O ALA C3015 2.215−9.497 1.761 1.00 26.98 O ATOM 1919 N SER C3016 3.683 −7.916 2.399 1.0026.19 N ATOM 1920 CA SER C3016 4.498 −8.062 1.192 1.00 27.18 C ATOM 1921CB SER C3016 5.706 −7.117 1.232 1.00 27.62 C ATOM 1922 OG SER C30165.324 −5.799 1.573 1.00 28.51 O ATOM 1923 C SER C3016 4.997 −9.502 1.0721.00 27.53 C ATOM 1924 O SER C3016 5.069 −10.062 −0.027 1.00 26.07 OATOM 1925 N ILE C3017 5.343 −10.094 2.212 1.00 26.80 N ATOM 1926 CA ILEC3017 5.841 −11.464 2.248 1.00 25.88 C ATOM 1927 CB ILE C3017 6.519−11.771 3.613 1.00 25.28 C ATOM 1928 CG2 ILE C3017 6.909 −13.241 3.6881.00 23.81 C ATOM 1929 CG1 ILE C3017 7.739 −10.863 3.808 1.00 24.39 CATOM 1930 CD1 ILE C3017 8.815 −11.007 2.735 1.00 24.49 C ATOM 1931 C ILEC3017 4.698 −12.456 2.019 1.00 26.06 C ATOM 1932 O ILE C3017 4.830−13.408 1.253 1.00 26.57 O ATOM 1933 N GLU C3018 3.576 −12.235 2.6901.00 26.59 N ATOM 1934 CA GLU C3018 2.429 −13.122 2.534 1.00 28.88 CATOM 1935 CB GLU C3018 1.284 −12.645 3.427 1.00 29.66 C ATOM 1936 CG GLUC3018 1.688 −12.504 4.884 1.00 32.78 C ATOM 1937 CD GLU C3018 0.656−11.783 5.722 1.00 34.19 C ATOM 1938 OE1 GLU C3018 −0.010 −10.865 5.1901.00 34.18 O ATOM 1939 OE2 GLU C3018 0.525 −12.118 6.920 1.00 35.99 OATOM 1940 C GLU C3018 1.983 −13.163 1.067 1.00 29.36 C ATOM 1941 O GLUC3018 1.763 −14.239 0.507 1.00 28.97 O ATOM 1942 N SER C3019 1.867−11.994 0.440 1.00 28.95 N ATOM 1943 CA SER C3019 1.454 −11.931 −0.9571.00 29.90 C ATOM 1944 CB SER C3019 1.285 −10.476 −1.410 1.00 30.07 CATOM 1945 OG SER C3019 2.542 −9.866 −1.632 1.00 33.15 O ATOM 1946 C SERC3019 2.489 −12.623 −1.837 1.00 30.43 C ATOM 1947 O SER C3019 2.138−13.362 −2.755 1.00 30.07 O ATOM 1948 N ALA C3020 3.766 −12.391 −1.5491.00 29.14 N ATOM 1949 CA ALA C3020 4.842 −12.994 −2.327 1.00 30.13 CATOM 1950 CB ALA C3020 6.191 −12.465 −1.847 1.00 31.02 C ATOM 1951 C ALAC3020 4.834 −14.527 −2.269 1.00 30.69 C ATOM 1952 O ALA C3020 5.111−15.198 −3.264 1.00 30.30 O ATOM 1953 N VAL C3021 4.530 −15.082 −1.1031.00 30.94 N ATOM 1954 CA VAL C3021 4.501 −16.532 −0.959 1.00 33.03 CATOM 1955 CB VAL C3021 4.172 −16.950 0.489 1.00 32.04 C ATOM 1956 CG1VAL C3021 3.982 −18.465 0.565 1.00 31.51 C ATOM 1957 CG2 VAL C3021 5.292−16.521 1.414 1.00 31.14 C ATOM 1958 C VAL C3021 3.458 −17.135 −1.8961.00 35.03 C ATOM 1959 O VAL C3021 3.736 −18.094 −2.616 1.00 36.27 OATOM 1960 N THR C3022 2.263 −16.552 −1.889 1.00 36.26 N ATOM 1961 CA THRC3022 1.166 −17.019 −2.726 1.00 38.71 C ATOM 1962 CB THR C3022 −0.142−16.274 −2.371 1.00 38.89 C ATOM 1963 OG1 THR C3022 −0.532 −16.613−1.034 1.00 39.61 O ATOM 1964 CG2 THR C3022 −1.262 −16.654 −3.336 1.0037.67 C ATOM 1965 C THR C3022 1.458 −16.836 −4.214 1.00 40.67 C ATOM1966 O THR C3022 1.325 −17.772 −5.005 1.00 40.21 O ATOM 1967 N ARG C30231.859 −15.626 −4.587 1.00 42.70 N ATOM 1968 CA ARG C3023 2.161 −15.303−5.974 1.00 46.22 C ATOM 1969 CB ARG C3023 2.861 −13.944 −6.037 1.0046.79 C ATOM 1970 CG ARG C3023 2.842 −13.278 −7.396 1.00 47.31 C ATOM1971 CD ARG C3023 3.264 −11.827 −7.269 1.00 47.58 C ATOM 1972 NE ARGC3023 4.544 −11.695 −6.577 1.00 48.02 N ATOM 1973 CZ ARG C3023 4.741−10.924 −5.511 1.00 48.91 C ATOM 1974 NH1 ARG C3023 3.736 −10.214 −5.0081.00 46.67 N ATOM 1975 NH2 ARG C3023 5.943 −10.861 −4.948 1.00 48.13 NATOM 1976 C ARG C3023 3.020 −16.391 −6.616 1.00 47.90 C ATOM 1977 O ARGC3023 2.684 −16.906 −7.681 1.00 49.41 O ATOM 1978 N HIS C3024 4.129−16.737 −5.968 1.00 49.64 N ATOM 1979 CA HIS C3024 5.019 −17.787 −6.4581.00 50.08 C ATOM 1980 CB HIS C3024 6.303 −17.193 −7.045 1.00 51.60 CATOM 1981 CG HIS C3024 6.100 −16.464 −8.338 1.00 53.54 C ATOM 1982 CD2HIS C3024 6.507 −16.754 −9.597 1.00 53.69 C ATOM 1983 ND1 HIS C30245.397 −15.282 −8.426 1.00 54.78 N ATOM 1984 CE1 HIS C3024 5.379 −14.875−9.683 1.00 53.97 C ATOM 1985 NE2 HIS C3024 6.045 −15.750 −10.414 1.0053.74 N ATOM 1986 C HIS C3024 5.370 −18.720 −5.304 1.00 50.32 C ATOM1987 O HIS C3024 6.030 −18.314 −4.347 1.00 50.15 O ATOM 1988 N GLU C30254.929 −19.971 −5.394 1.00 49.54 N ATOM 1989 CA GLU C3025 5.197 −20.937−4.335 1.00 49.18 C ATOM 1990 CB GLU C3025 4.507 −22.270 −4.632 1.0052.19 C ATOM 1991 CG GLU C3025 4.778 −23.331 −3.575 1.00 55.07 C ATOM1992 CD GLU C3025 4.269 −24.694 −3.972 1.00 57.92 C ATOM 1993 OE1 GLUC3025 3.033 −24.870 −4.053 1.00 58.55 O ATOM 1994 OE2 GLU C3025 5.111−25.590 −4.206 1.00 59.67 O ATOM 1995 C GLU C3025 6.685 −21.182 −4.1181.00 46.90 C ATOM 1996 O GLU C3025 7.087 −21.711 −3.084 1.00 47.27 OATOM 1997 N GLY C3026 7.502 −20.801 −5.092 1.00 44.54 N ATOM 1998 CA GLYC3026 8.933 −20.997 −4.956 1.00 41.90 C ATOM 1999 C GLY C3026 9.636−19.811 −4.320 1.00 40.26 C ATOM 2000 O GLY C3026 10.867 −19.768 −4.2651.00 39.86 O ATOM 2001 N PHE C3027 8.860 −18.842 −3.841 1.00 37.59 NATOM 2002 CA PHE C3027 9.434 −17.655 −3.217 1.00 35.31 C ATOM 2003 CBPHE C3027 8.323 −16.715 −2.738 1.00 34.09 C ATOM 2004 CG PHE C3027 8.832−15.491 −2.031 1.00 33.77 C ATOM 2005 CD1 PHE C3027 9.633 −14.569 −2.7001.00 33.43 C ATOM 2006 CD2 PHE C3027 8.543 −15.277 −0.687 1.00 32.68 CATOM 2007 CE1 PHE C3027 10.141 −13.450 −2.042 1.00 32.28 C ATOM 2008 CE2PHE C3027 9.045 −14.163 −0.016 1.00 33.06 C ATOM 2009 CZ PHE C3027 9.847−13.248 −0.696 1.00 33.30 C ATOM 2010 C PHE C3027 10.331 −18.032 −2.0421.00 34.03 C ATOM 2011 O PHE C3027 11.511 −17.688 −2.019 1.00 34.88 OATOM 2012 N ALA C3028 9.767 −18.743 −1.071 1.00 33.39 N ATOM 2013 CA ALAC3028 10.516 −19.159 0.109 1.00 34.32 C ATOM 2014 CB ALA C3028 9.651−20.053 0.987 1.00 33.64 C ATOM 2015 C ALA C3028 11.799 −19.885 −0.2631.00 34.75 C ATOM 2016 O ALA C3028 12.873 −19.572 0.257 1.00 34.90 OATOM 2017 N LYS C3029 11.683 −20.854 −1.166 1.00 33.73 N ATOM 2018 CALYS C3029 12.831 −21.636 −1.605 1.00 32.87 C ATOM 2019 CB LYS C302912.396 −22.671 −2.650 1.00 32.28 C ATOM 2020 CG LYS C3029 11.313 −23.617−2.157 0.05 32.40 C ATOM 2021 CD LYS C3029 10.821 −24.537 −3.261 0.0532.28 C ATOM 2022 CE LYS C3029 9.721 −25.456 −2.753 0.05 32.20 C ATOM2023 NZ LYS C3029 9.160 −26.313 −3.833 0.05 32.15 N ATOM 2024 C LYSC3029 13.910 −20.735 −2.181 1.00 32.70 C ATOM 2025 O LYS C3029 15.100−21.016 −2.048 1.00 33.44 O ATOM 2026 N ARG C3030 13.498 −19.643 −2.8141.00 32.85 N ATOM 2027 CA ARG C3030 14.458 −18.714 −3.397 1.00 32.53 CATOM 2028 CB ARG C3030 13.796 −17.877 −4.497 0.05 32.58 C ATOM 2029 CGARG C3030 13.442 −18.670 −5.747 0.05 32.72 C ATOM 2030 CD ARG C303013.135 −17.752 −6.922 0.05 32.87 C ATOM 2031 NE ARG C3030 11.916 −16.973−6.722 0.05 33.03 N ATOM 2032 CZ ARG C3030 10.691 −17.490 −6.720 0.0533.10 C ATOM 2033 NH1 ARG C3030 10.517 −18.791 −6.908 0.05 33.16 N ATOM2034 NH2 ARG C3030 9.639 −16.705 −6.531 0.05 33.04 N ATOM 2035 C ARGC3030 15.080 −17.794 −2.351 1.00 32.30 C ATOM 2036 O ARG C3030 16.242−17.408 −2.470 1.00 32.85 O ATOM 2037 N VAL C3031 14.303 −17.455 −1.3251.00 31.53 N ATOM 2038 CA VAL C3031 14.755 −16.574 −0.245 1.00 30.10 CATOM 2039 CB VAL C3031 13.541 −15.905 0.469 1.00 30.44 C ATOM 2040 CG1VAL C3031 14.007 −15.140 1.701 1.00 31.92 C ATOM 2041 CG2 VAL C303112.824 −14.967 −0.484 1.00 31.35 C ATOM 2042 C VAL C3031 15.576 −17.2840.836 1.00 29.72 C ATOM 2043 O VAL C3031 16.475 −16.686 1.439 1.00 29.40O ATOM 2044 N LEU C3032 15.259 −18.554 1.076 1.00 27.31 N ATOM 2045 CALEU C3032 15.911 −19.338 2.119 1.00 25.97 C ATOM 2046 CB LEU C303214.839 −19.917 3.047 1.00 24.74 C ATOM 2047 CG LEU C3032 13.782 −18.9433.572 1.00 22.82 C ATOM 2048 CD1 LEU C3032 12.717 −19.708 4.361 1.0023.17 C ATOM 2049 CD2 LEU C3032 14.454 −17.893 4.452 1.00 21.55 C ATOM2050 C LEU C3032 16.793 −20.485 1.630 1.00 27.28 C ATOM 2051 O LEU C303216.447 −21.187 0.676 1.00 28.34 O ATOM 2052 N THR C3033 17.924 −20.6762.307 1.00 26.40 N ATOM 2053 CA THR C3033 18.847 −21.756 1.984 1.0027.30 C ATOM 2054 CB THR C3033 20.149 −21.662 2.795 1.00 25.69 C ATOM2055 OG1 THR C3033 19.845 −21.820 4.186 1.00 26.34 O ATOM 2056 CG2 THRC3033 20.835 −20.323 2.574 1.00 26.77 C ATOM 2057 C THR C3033 18.170−23.062 2.385 1.00 27.70 C ATOM 2058 O THR C3033 17.061 −23.061 2.9201.00 28.12 O ATOM 2059 N ALA C3034 18.853 −24.174 2.145 1.00 28.90 NATOM 2060 CA ALA C3034 18.314 −25.484 2.493 1.00 29.05 C ATOM 2061 CBALA C3034 19.283 −26.572 2.062 1.00 29.42 C ATOM 2062 C ALA C3034 18.047−25.594 3.990 1.00 28.60 C ATOM 2063 O ALA C3034 16.965 −26.008 4.4031.00 29.51 O ATOM 2064 N LEU C3035 19.029 −25.218 4.805 1.00 28.04 NATOM 2065 CA LEU C3035 18.869 −25.310 6.249 1.00 27.61 C ATOM 2066 CBLEU C3035 20.187 −24.964 6.952 1.00 29.31 C ATOM 2067 CG LEU C303520.522 −25.809 8.190 1.00 31.59 C ATOM 2068 CD1 LEU C3035 20.472 −27.2977.821 1.00 32.29 C ATOM 2069 CD2 LEU C3035 21.902 −25.438 8.727 1.0030.00 C ATOM 2070 C LEU C3035 17.740 −24.410 6.747 1.00 27.52 C ATOM2071 O LEU C3035 16.922 −24.832 7.571 1.00 26.23 O ATOM 2072 N GLU C303617.688 −23.176 6.247 1.00 27.39 N ATOM 2073 CA GLU C3036 16.636 −22.2406.649 1.00 27.23 C ATOM 2074 CB GLU C3036 16.849 −20.877 5.981 1.0025.56 C ATOM 2075 CG GLU C3036 17.834 −19.978 6.707 1.00 22.65 C ATOM2076 CD GLU C3036 18.256 −18.777 5.880 1.00 23.21 C ATOM 2077 OE1 GLUC3036 18.735 −17.784 6.469 1.00 22.56 O ATOM 2078 OE2 GLU C3036 18.124−18.825 4.638 1.00 24.80 O ATOM 2079 C GLU C3036 15.258 −22.793 6.2781.00 28.00 C ATOM 2080 O GLU C3036 14.306 −22.668 7.047 1.00 27.30 OATOM 2081 N MET C3037 15.160 −23.401 5.098 1.00 28.24 N ATOM 2082 CA METC3037 13.897 −23.979 4.641 1.00 30.24 C ATOM 2083 CB MET C3037 14.051−24.593 3.247 1.00 31.74 C ATOM 2084 CG MET C3037 13.885 −23.605 2.1021.00 32.56 C ATOM 2085 SD MET C3037 12.289 −22.761 2.156 1.00 37.45 SATOM 2086 CE MET C3037 11.153 −24.108 1.753 1.00 36.07 C ATOM 2087 C METC3037 13.411 −25.049 5.608 1.00 31.16 C ATOM 2088 O MET C3037 12.222−25.124 5.920 1.00 30.55 O ATOM 2089 N GLU C3038 14.336 −25.882 6.0761.00 31.23 N ATOM 2090 CA GLU C3038 13.992 −26.936 7.018 1.00 31.35 CATOM 2091 CB GLU C3038 15.257 −27.635 7.525 0.05 30.95 C ATOM 2092 CGGLU C3038 15.478 −29.023 6.948 0.05 30.58 C ATOM 2093 CD GLU C303816.721 −29.692 7.504 0.05 30.41 C ATOM 2094 OE1 GLU C3038 16.840 −29.7958.744 0.05 30.03 O ATOM 2095 OE2 GLU C3038 17.578 −30.118 6.702 0.0530.15 O ATOM 2096 C GLU C3038 13.235 −26.330 8.191 1.00 31.53 C ATOM2097 O GLU C3038 12.255 −26.897 8.663 1.00 32.15 O ATOM 2098 N ARG C303913.697 −25.176 8.664 1.00 32.00 N ATOM 2099 CA ARG C3039 13.046 −24.4969.781 1.00 33.21 C ATOM 2100 CB ARG C3039 13.928 −23.353 10.289 1.0034.11 C ATOM 2101 CG ARG C3039 13.317 −22.548 11.434 1.00 37.68 C ATOM2102 CD ARG C3039 13.189 −23.377 12.704 1.00 39.59 C ATOM 2103 NE ARGC3039 12.565 −22.626 13.791 1.00 41.92 N ATOM 2104 CZ ARG C3039 12.195−23.159 14.952 1.00 43.02 C ATOM 2105 NH1 ARG C3039 12.384 −24.45015.183 1.00 43.57 N ATOM 2106 NH2 ARG C3039 11.625 −22.402 15.881 1.0044.00 N ATOM 2107 C ARG C3039 11.692 −23.939 9.339 1.00 32.70 C ATOM2108 O ARG C3039 10.674 −24.130 10.005 1.00 31.81 O ATOM 2109 N PHEC3040 11.699 −23.240 8.210 1.00 32.86 N ATOM 2110 CA PHE C3040 10.489−22.646 7.653 1.00 33.52 C ATOM 2111 CB PHE C3040 10.778 −22.128 6.2421.00 32.08 C ATOM 2112 CG PHE C3040 9.569 −21.604 5.528 1.00 32.50 CATOM 2113 CD1 PHE C3040 9.012 −20.380 5.880 1.00 31.27 C ATOM 2114 CD2PHE C3040 8.980 −22.340 4.503 1.00 32.76 C ATOM 2115 CE1 PHE C3040 7.882−19.895 5.222 1.00 31.92 C ATOM 2116 CE2 PHE C3040 7.851 −21.865 3.8391.00 33.27 C ATOM 2117 CZ PHE C3040 7.301 −20.637 4.201 1.00 31.45 CATOM 2118 C PHE C3040 9.367 −23.680 7.595 1.00 33.45 C ATOM 2119 O PHEC3040 8.264 −23.457 8.100 1.00 33.35 O ATOM 2120 N THR C3041 9.669−24.819 6.983 1.00 34.68 N ATOM 2121 CA THR C3041 8.706 −25.898 6.8281.00 35.57 C ATOM 2122 CB THR C3041 9.286 −27.002 5.923 1.00 36.24 CATOM 2123 OG1 THR C3041 9.517 −26.464 4.616 1.00 38.04 O ATOM 2124 CG2THR C3041 8.324 −28.170 5.813 1.00 36.60 C ATOM 2125 C THR C3041 8.232−26.517 8.143 1.00 36.09 C ATOM 2126 O THR C3041 7.084 −26.945 8.2471.00 37.27 O ATOM 2127 N SER C3042 9.100 −26.560 9.147 1.00 36.67 N ATOM2128 CA SER C3042 8.718 −27.142 10.427 1.00 37.38 C ATOM 2129 CB SERC3042 9.952 −27.377 11.303 1.00 38.44 C ATOM 2130 OG SER C3042 10.391−26.172 11.904 1.00 39.31 O ATOM 2131 C SER C3042 7.744 −26.230 11.1571.00 37.81 C ATOM 2132 O SER C3042 7.010 −26.671 12.042 1.00 38.07 OATOM 2133 N LEU C3043 7.740 −24.956 10.781 1.00 37.43 N ATOM 2134 CA LEUC3043 6.860 −23.969 11.400 1.00 37.02 C ATOM 2135 CB LEU C3043 7.549−22.600 11.428 1.00 37.05 C ATOM 2136 CG LEU C3043 8.597 −22.327 12.5131.00 37.93 C ATOM 2137 CD1 LEU C3043 9.573 −23.470 12.628 1.00 39.39 CATOM 2138 CD2 LEU C3043 9.328 −21.040 12.177 1.00 38.02 C ATOM 2139 CLEU C3043 5.526 −23.851 10.666 1.00 37.04 C ATOM 2140 O LEU C3043 5.389−24.291 9.522 1.00 37.65 O ATOM 2141 N LYS C3044 4.542 −23.250 11.3251.00 36.12 N ATOM 2142 CA LYS C3044 3.236 −23.075 10.707 1.00 35.63 CATOM 2143 CB LYS C3044 2.313 −24.246 11.072 1.00 37.63 C ATOM 2144 CGLYS C3044 1.985 −24.356 12.555 1.00 40.09 C ATOM 2145 CD LYS C3044 0.926−25.432 12.813 1.00 42.38 C ATOM 2146 CE LYS C3044 1.397 −26.813 12.3651.00 42.85 C ATOM 2147 NZ LYS C3044 0.339 −27.847 12.550 1.00 43.11 NATOM 2148 C LYS C3044 2.584 −21.753 11.111 1.00 33.57 C ATOM 2149 O LYSC3044 2.990 −21.116 12.086 1.00 33.02 O ATOM 2150 N GLY C3045 1.579−21.345 10.339 1.00 31.64 N ATOM 2151 CA GLY C3045 0.860 −20.115 10.6181.00 29.90 C ATOM 2152 C GLY C3045 1.689 −18.844 10.666 1.00 28.38 CATOM 2153 O GLY C3045 2.643 −18.676 9.915 1.00 28.13 O ATOM 2154 N ARGC3046 1.299 −17.946 11.564 1.00 28.66 N ATOM 2155 CA ARG C3046 1.957−16.661 11.758 1.00 27.23 C ATOM 2156 CB ARG C3046 1.279 −15.920 12.9120.05 27.45 C ATOM 2157 CG ARG C3046 −0.235 −15.860 12.769 0.05 27.80 CATOM 2158 CD ARG C3046 −0.912 −15.403 14.048 0.05 28.08 C ATOM 2159 NEARG C3046 −2.364 −15.526 13.962 0.05 28.35 N ATOM 2160 CZ ARG C3046−3.199 −15.249 14.959 0.05 28.51 C ATOM 2161 NH1 ARG C3046 −4.506−15.394 14.792 0.05 28.59 N ATOM 2162 NH2 ARG C3046 −2.727 −14.83116.127 0.05 28.63 N ATOM 2163 C ARG C3046 3.451 −16.827 12.041 1.0026.66 C ATOM 2164 O ARG C3046 4.276 −16.065 11.537 1.00 23.83 O ATOM2165 N ARG C3047 3.797 −17.824 12.847 1.00 26.74 N ATOM 2166 CA ARGC3047 5.197 −18.068 13.172 1.00 28.45 C ATOM 2167 CB ARG C3047 5.330−19.223 14.167 1.00 30.78 C ATOM 2168 CG ARG C3047 4.824 −18.919 15.5671.00 36.74 C ATOM 2169 CD ARG C3047 5.548 −19.793 16.580 1.00 40.75 CATOM 2170 NE ARG C3047 6.991 −19.561 16.540 1.00 43.99 N ATOM 2171 CZARG C3047 7.894 −20.341 17.126 1.00 45.84 C ATOM 2172 NH1 ARG C30477.508 −21.417 17.803 1.00 47.05 N ATOM 2173 NH2 ARG C3047 9.184 −20.04617.036 1.00 46.26 N ATOM 2174 C ARG C3047 6.004 −18.396 11.924 1.0026.96 C ATOM 2175 O ARG C3047 7.171 −18.019 11.809 1.00 27.18 O ATOM2176 N GLN C3048 5.385 −19.108 10.989 1.00 25.16 N ATOM 2177 CA GLNC3048 6.080 −19.474 9.765 1.00 24.64 C ATOM 2178 CB GLN C3048 5.262−20.489 8.964 1.00 24.71 C ATOM 2179 CG GLN C3048 6.087 −21.176 7.8841.00 24.87 C ATOM 2180 CD GLN C3048 5.261 −22.028 6.947 1.00 27.10 CATOM 2181 OE1 GLN C3048 5.757 −23.007 6.393 1.00 28.27 O ATOM 2182 NE2GLN C3048 4.000 −21.650 6.747 1.00 27.28 N ATOM 2183 C GLN C3048 6.342−18.240 8.907 1.00 23.81 C ATOM 2184 O GLN C3048 7.441 −18.064 8.3761.00 22.00 O ATOM 2185 N ILE C3049 5.323 −17.394 8.767 1.00 23.83 N ATOM2186 CA ILE C3049 5.449 −16.174 7.972 1.00 22.84 C ATOM 2187 CB ILEC3049 4.099 −15.428 7.889 1.00 23.39 C ATOM 2188 CG2 ILE C3049 4.270−14.110 7.123 1.00 20.78 C ATOM 2189 CG1 ILE C3049 3.068 −16.317 7.1941.00 25.01 C ATOM 2190 CD1 ILE C3049 1.637 −15.812 7.313 1.00 28.28 CATOM 2191 C ILE C3049 6.492 −15.254 8.596 1.00 22.76 C ATOM 2192 O ILEC3049 7.334 −14.695 7.901 1.00 22.64 O ATOM 2193 N GLU C3050 6.426−15.119 9.917 1.00 23.06 N ATOM 2194 CA GLU C3050 7.347 −14.287 10.6851.00 23.40 C ATOM 2195 CB GLU C3050 7.023 −14.436 12.169 1.00 27.99 CATOM 2196 CG GLU C3050 7.336 −13.229 13.014 1.00 34.34 C ATOM 2197 CDGLU C3050 6.633 −11.997 12.501 1.00 37.30 C ATOM 2198 OE1 GLU C30507.273 −11.233 11.752 1.00 38.54 O ATOM 2199 OE2 GLU C3050 5.437 −11.80712.825 1.00 38.13 O ATOM 2200 C GLU C3050 8.798 −14.707 10.429 1.0022.91 C ATOM 2201 O GLU C3050 9.675 −13.863 10.212 1.00 19.78 O ATOM2202 N TYR C3051 9.042 −16.018 10.451 1.00 20.98 N ATOM 2203 CA TYRC3051 10.379 −16.549 10.218 1.00 20.96 C ATOM 2204 CB TYR C3051 10.376−18.087 10.286 1.00 20.94 C ATOM 2205 CG TYR C3051 11.727 −18.710 9.9961.00 21.84 C ATOM 2206 CD1 TYR C3051 12.091 −19.072 8.699 1.00 21.88 CATOM 2207 CE1 TYR C3051 13.365 −19.563 8.420 1.00 22.08 C ATOM 2208 CD2TYR C3051 12.675 −18.864 11.011 1.00 24.22 C ATOM 2209 CE2 TYR C305113.947 −19.353 10.743 1.00 22.50 C ATOM 2210 CZ TYR C3051 14.286 −19.6959.447 1.00 23.28 C ATOM 2211 OH TYR C3051 15.557 −20.142 9.181 1.0026.17 O ATOM 2212 C TYR C3051 10.893 −16.093 8.863 1.00 21.41 C ATOM2213 O TYR C3051 11.973 −15.508 8.764 1.00 20.67 O ATOM 2214 N LEU C305210.104 −16.357 7.823 1.00 20.18 N ATOM 2215 CA LEU C3052 10.468 −15.9856.465 1.00 19.73 C ATOM 2216 CB LEU C3052 9.347 −16.399 5.502 1.00 20.90C ATOM 2217 CG LEU C3052 9.488 −16.052 4.019 1.00 20.73 C ATOM 2218 CD1LEU C3052 10.837 −16.537 3.484 1.00 21.92 C ATOM 2219 CD2 LEU C30528.329 −16.704 3.247 1.00 22.34 C ATOM 2220 C LEU C3052 10.725 −14.4876.365 1.00 18.62 C ATOM 2221 O LEU C3052 11.745 −14.057 5.819 1.00 18.97O ATOM 2222 N ALA C3053 9.805 −13.697 6.912 1.00 18.23 N ATOM 2223 CAALA C3053 9.921 −12.238 6.888 1.00 19.28 C ATOM 2224 CB ALA C3053 8.670−11.611 7.489 1.00 19.78 C ATOM 2225 C ALA C3053 11.164 −11.746 7.6341.00 18.63 C ATOM 2226 O ALA C3053 11.835 −10.815 7.191 1.00 17.69 OATOM 2227 N GLY C3054 11.464 −12.375 8.767 1.00 18.30 N ATOM 2228 CA GLYC3054 12.635 −11.989 9.534 1.00 18.14 C ATOM 2229 C GLY C3054 13.915−12.303 8.776 1.00 19.55 C ATOM 2230 O GLY C3054 14.888 −11.545 8.8311.00 18.40 O ATOM 2231 N ARG C3055 13.927 −13.421 8.060 1.00 18.30 NATOM 2232 CA ARG C3055 15.112 −13.783 7.298 1.00 19.48 C ATOM 2233 CBARG C3055 15.021 −15.239 6.839 1.00 20.53 C ATOM 2234 CG ARG C305515.815 −16.213 7.709 1.00 22.48 C ATOM 2235 CD ARG C3055 15.450 −16.0939.181 1.00 26.13 C ATOM 2236 NE ARG C3055 16.291 −16.945 10.019 1.0028.05 N ATOM 2237 CZ ARG C3055 16.240 −16.972 11.347 1.00 28.02 C ATOM2238 NH1 ARG C3055 15.389 −16.190 11.999 1.00 28.89 N ATOM 2239 NH2 ARGC3055 17.034 −17.788 12.024 1.00 28.23 N ATOM 2240 C ARG C3055 15.283−12.849 6.108 1.00 20.40 C ATOM 2241 O ARG C3055 16.396 −12.399 5.8171.00 20.36 O ATOM 2242 N TRP C3056 14.182 −12.547 5.424 1.00 20.72 NATOM 2243 CA TRP C3056 14.234 −11.641 4.280 1.00 22.18 C ATOM 2244 CBTRP C3056 12.837 −11.486 3.655 1.00 23.99 C ATOM 2245 CG TRP C305612.716 −10.303 2.719 1.00 29.31 C ATOM 2246 CD2 TRP C3056 12.723 −10.3351.289 1.00 30.25 C ATOM 2247 CE2 TRP C3056 12.609 −9.001 0.840 1.0032.03 C ATOM 2248 CE3 TRP C3056 12.821 −11.362 0.342 1.00 33.18 C ATOM2249 CD1 TRP C3056 12.598 −8.984 3.070 1.00 30.82 C ATOM 2250 NE1 TRPC3056 12.532 −8.198 1.947 1.00 33.62 N ATOM 2251 CZ2 TRP C3056 12.582−8.665 −0.515 1.00 34.74 C ATOM 2252 CZ3 TRP C3056 12.795 −11.029 −1.0101.00 34.82 C ATOM 2253 CH2 TRP C3056 12.679 −9.690 −1.425 1.00 36.26 CATOM 2254 C TRP C3056 14.746 −10.284 4.760 1.00 20.86 C ATOM 2255 O TRPC3056 15.608 −9.670 4.134 1.00 18.98 O ATOM 2256 N SER C3057 14.206−9.835 5.885 1.00 18.95 N ATOM 2257 CA SER C3057 14.586 −8.558 6.4871.00 19.90 C ATOM 2258 CB SER C3057 13.755 −8.321 7.752 1.00 21.78 CATOM 2259 OG SER C3057 14.067 −7.076 8.342 1.00 25.39 O ATOM 2260 C SERC3057 16.070 −8.506 6.841 1.00 18.84 C ATOM 2261 O SER C3057 16.767−7.545 6.514 1.00 19.51 O ATOM 2262 N ALA C3058 16.550 −9.545 7.509 1.0018.85 N ATOM 2263 CA ALA C3058 17.949 −9.611 7.917 1.00 18.94 C ATOM2264 CB ALA C3058 18.182 −10.854 8.765 1.00 16.86 C ATOM 2265 C ALAC3058 18.912 −9.608 6.730 1.00 19.28 C ATOM 2266 O ALA C3058 19.955−8.946 6.765 1.00 19.47 O ATOM 2267 N LYS C3059 18.567 −10.349 5.6831.00 18.93 N ATOM 2268 CA LYS C3059 19.424 −10.432 4.507 1.00 19.60 CATOM 2269 CB LYS C3059 18.965 −11.575 3.604 1.00 20.15 C ATOM 2270 CGLYS C3059 19.102 −12.925 4.271 1.00 17.40 C ATOM 2271 CD LYS C305918.773 −14.069 3.331 1.00 21.58 C ATOM 2272 CE LYS C3059 18.813 −15.3924.070 1.00 19.13 C ATOM 2273 NZ LYS C3059 18.667 −16.545 3.158 1.0024.92 N ATOM 2274 C LYS C3059 19.437 −9.121 3.744 1.00 21.37 C ATOM 2275O LYS C3059 20.457 −8.734 3.165 1.00 22.73 O ATOM 2276 N GLU C306018.297 −8.440 3.745 1.00 22.26 N ATOM 2277 CA GLU C3060 18.175 −7.1583.080 1.00 22.29 C ATOM 2278 CB GLU C3060 16.708 −6.716 3.076 1.00 24.97C ATOM 2279 CG GLU C3060 16.424 −5.392 2.373 1.00 32.66 C ATOM 2280 CDGLU C3060 16.807 −5.410 0.901 1.00 37.10 C ATOM 2281 OE1 GLU C306016.401 −6.359 0.190 1.00 38.38 O ATOM 2282 OE2 GLU C3060 17.509 −4.4720.456 1.00 38.70 O ATOM 2283 C GLU C3060 19.042 −6.172 3.864 1.00 20.94C ATOM 2284 O GLU C3060 19.829 −5.429 3.285 1.00 22.93 O ATOM 2285 N ALAC3061 18.907 −6.178 5.186 1.00 19.68 N ATOM 2286 CA ALA C3061 19.698−5.282 6.024 1.00 20.17 C ATOM 2287 CB ALA C3061 19.373 −5.515 7.4991.00 19.49 C ATOM 2288 C ALA C3061 21.185 −5.520 5.759 1.00 19.14 C ATOM2289 O ALA C3061 21.953 −4.576 5.572 1.00 18.81 O ATOM 2290 N PHE C306221.588 −6.786 5.723 1.00 19.90 N ATOM 2291 CA PHE C3062 22.987 −7.1155.465 1.00 19.78 C ATOM 2292 CB PHE C3062 23.214 −8.624 5.570 1.00 20.80C ATOM 2293 CG PHE C3062 24.604 −9.051 5.171 1.00 21.17 C ATOM 2294 CD1PHE C3062 24.896 −9.376 3.847 1.00 21.25 C ATOM 2295 CD2 PHE C306225.629 −9.074 6.109 1.00 20.45 C ATOM 2296 CE1 PHE C3062 26.195 −9.7173.463 1.00 22.31 C ATOM 2297 CE2 PHE C3062 26.930 −9.412 5.738 1.0021.98 C ATOM 2298 CZ PHE C3062 27.211 −9.733 4.410 1.00 22.06 C ATOM2299 C PHE C3062 23.443 −6.629 4.089 1.00 21.35 C ATOM 2300 O PHE C306224.526 −6.067 3.951 1.00 20.77 O ATOM 2301 N SER C3063 22.612 −6.8433.074 1.00 22.17 N ATOM 2302 CA SER C3063 22.949 −6.434 1.717 1.00 22.74C ATOM 2303 CB SER C3063 21.851 −6.873 0.754 1.00 23.43 C ATOM 2304 OGSER C3063 21.635 −8.265 0.877 1.00 28.48 O ATOM 2305 C SER C3063 23.123−4.926 1.649 1.00 22.84 C ATOM 2306 O SER C3063 24.001 −4.422 0.947 1.0021.58 O ATOM 2307 N LYS C3064 22.277 −4.205 2.377 1.00 21.35 N ATOM 2308CA LYS C3064 22.370 −2.755 2.406 1.00 21.55 C ATOM 2309 CB LYS C306421.111 −2.168 3.055 1.00 22.13 C ATOM 2310 CG LYS C3064 19.841 −2.4162.238 1.00 21.86 C ATOM 2311 CD LYS C3064 18.588 −1.884 2.929 1.00 22.40C ATOM 2312 CE LYS C3064 18.653 −0.375 3.120 1.00 22.07 C ATOM 2313 NZLYS C3064 17.579 0.125 4.017 1.00 21.49 N ATOM 2314 C LYS C3064 23.639−2.341 3.168 1.00 21.95 C ATOM 2315 O LYS C3064 24.295 −1.363 2.812 1.0022.05 O ATOM 2316 N ALA C3065 23.994 −3.104 4.197 1.00 20.93 N ATOM 2317CA ALA C3065 25.193 −2.818 4.983 1.00 23.70 C ATOM 2318 CB ALA C306525.254 −3.729 6.200 1.00 22.08 C ATOM 2319 C ALA C3065 26.450 −3.0104.136 1.00 25.75 C ATOM 2320 O ALA C3065 27.420 −2.278 4.297 1.00 25.29O ATOM 2321 N MET C3066 26.433 −4.008 3.255 1.00 27.80 N ATOM 2322 CAMET C3066 27.569 −4.278 2.375 1.00 31.06 C ATOM 2323 CB MET C3066 27.386−5.616 1.649 1.00 30.03 C ATOM 2324 CG MET C3066 27.666 −6.848 2.4951.00 30.77 C ATOM 2325 SD MET C3066 29.395 −6.944 3.059 1.00 31.09 SATOM 2326 CE MET C3066 30.192 −7.610 1.576 1.00 29.01 C ATOM 2327 C METC3066 27.683 −3.159 1.342 1.00 33.44 C ATOM 2328 O MET C3066 28.778−2.782 0.940 1.00 32.94 O ATOM 2329 N GLY C3067 26.539 −2.634 0.918 1.0036.57 N ATOM 2330 CA GLY C3067 26.542 −1.565 −0.059 1.00 40.47 C ATOM2331 C GLY C3067 26.101 −2.041 −1.426 1.00 43.36 C ATOM 2332 O GLY C306726.602 −1.573 −2.447 1.00 44.87 O ATOM 2333 N THR C3068 25.161 −2.976−1.447 0.05 44.27 N ATOM 2334 CA THR C3068 24.650 −3.506 −2.701 0.0545.40 C ATOM 2335 CB THR C3068 25.521 −4.680 −3.201 0.05 45.40 C ATOM2336 OG1 THR C3068 25.018 −5.147 −4.459 0.05 45.48 O ATOM 2337 CG2 THRC3068 25.518 −5.821 −2.193 0.05 45.43 C ATOM 2338 C THR C3068 23.212−3.973 −2.507 0.05 46.15 C ATOM 2339 O THR C3068 22.452 −3.355 −1.7610.05 46.24 O ATOM 2340 N GLY C3069 22.839 −5.058 −3.175 0.05 47.05 NATOM 2341 CA GLY C3069 21.488 −5.567 −3.043 0.05 48.19 C ATOM 2342 C GLYC3069 21.341 −6.984 −3.555 0.05 48.95 C ATOM 2343 O GLY C3069 22.322−7.627 −3.927 0.05 49.00 O ATOM 2344 N ILE C3070 20.106 −7.471 −3.5690.05 49.77 N ATOM 2345 CA ILE C3070 19.809 −8.817 −4.038 0.05 50.58 CATOM 2346 CB ILE C3070 18.311 −9.155 −3.800 0.05 50.80 C ATOM 2347 CG2ILE C3070 17.434 −8.193 −4.584 0.05 51.01 C ATOM 2348 CG1 ILE C307018.011 −10.600 −4.205 0.05 51.05 C ATOM 2349 CD1 ILE C3070 18.852−11.631 −3.486 0.05 51.19 C ATOM 2350 C ILE C3070 20.140 −8.927 −5.5280.05 50.91 C ATOM 2351 O ILE C3070 20.642 −7.977 −6.126 0.05 50.98 OATOM 2352 N SER C3071 19.868 −10.093 −6.108 0.05 51.31 N ATOM 2353 CASER C3071 20.112 −10.372 −7.522 0.05 51.63 C ATOM 2354 CB SER C307119.393 −9.349 −8.411 0.05 51.73 C ATOM 2355 OG SER C3071 20.018 −8.080−8.363 0.05 51.85 O ATOM 2356 C SER C3071 21.592 −10.420 −7.891 0.0551.76 C ATOM 2357 O SER C3071 21.967 −11.053 −8.878 0.05 51.87 O ATOM2358 N LYS C3072 22.433 −9.755 −7.106 0.05 51.86 N ATOM 2359 CA LYSC3072 23.867 −9.751 −7.374 0.05 51.85 C ATOM 2360 CB LYS C3072 24.396−8.312 −7.449 0.05 52.23 C ATOM 2361 CG LYS C3072 24.392 −7.543 −6.1310.05 52.70 C ATOM 2362 CD LYS C3072 25.580 −7.907 −5.245 0.05 53.07 CATOM 2363 CE LYS C3072 26.905 −7.581 −5.920 0.05 53.33 C ATOM 2364 NZLYS C3072 27.022 −6.134 −6.253 0.05 53.48 N ATOM 2365 C LYS C3072 24.606−10.529 −6.292 0.05 51.55 C ATOM 2366 O LYS C3072 25.643 −11.140 −6.5500.05 51.64 O ATOM 2367 N LEU C3073 24.062 −10.500 −5.080 0.05 51.11 NATOM 2368 CA LEU C3073 24.660 −11.204 −3.953 0.05 50.57 C ATOM 2369 CBLEU C3073 24.615 −10.328 −2.699 0.05 50.79 C ATOM 2370 CG LEU C307325.349 −10.863 −1.467 0.05 50.92 C ATOM 2371 CD1 LEU C3073 26.830−11.010 −1.783 0.05 51.03 C ATOM 2372 CD2 LEU C3073 25.145 −9.917 −0.2940.05 50.94 C ATOM 2373 C LEU C3073 23.893 −12.498 −3.707 0.05 50.00 CATOM 2374 O LEU C3073 24.444 −13.473 −3.198 0.05 50.02 O ATOM 2375 N GLYC3074 22.616 −12.492 −4.076 1.00 49.38 N ATOM 2376 CA GLY C3074 21.779−13.663 −3.899 1.00 48.02 C ATOM 2377 C GLY C3074 21.479 −13.986 −2.4471.00 46.92 C ATOM 2378 O GLY C3074 22.391 −14.150 −1.642 1.00 46.73 OATOM 2379 N PHE C3075 20.197 −14.076 −2.107 1.00 46.04 N ATOM 2380 CAPHE C3075 19.804 −14.393 −0.741 1.00 45.56 C ATOM 2381 CB PHE C307518.305 −14.137 −0.544 1.00 45.22 C ATOM 2382 CG PHE C3075 17.969 −12.705−0.211 1.00 44.58 C ATOM 2383 CD1 PHE C3075 18.961 −11.724 −0.187 1.0044.91 C ATOM 2384 CD2 PHE C3075 16.661 −12.337 0.082 1.00 43.89 C ATOM2385 CE1 PHE C3075 18.654 −10.397 0.127 1.00 45.66 C ATOM 2386 CE2 PHEC3075 16.340 −11.016 0.398 1.00 44.22 C ATOM 2387 CZ PHE C3075 17.338−10.042 0.420 1.00 44.74 C ATOM 2388 C PHE C3075 20.147 −15.841 −0.4071.00 45.42 C ATOM 2389 O PHE C3075 20.099 −16.251 0.754 1.00 44.99 OATOM 2390 N GLN C3076 20.503 −16.607 −1.433 1.00 44.83 N ATOM 2391 CAGLN C3076 20.874 −18.006 −1.256 1.00 44.38 C ATOM 2392 CB GLN C307620.766 −18.749 −2.589 1.00 44.21 C ATOM 2393 CG GLN C3076 19.360 −19.192−2.890 1.00 45.02 C ATOM 2394 CD GLN C3076 18.868 −20.206 −1.880 1.0046.01 C ATOM 2395 OE1 GLN C3076 17.666 −20.367 −1.676 1.00 47.94 O ATOM2396 NE2 GLN C3076 19.802 −20.906 −1.245 1.00 45.65 N ATOM 2397 C GLNC3076 22.287 −18.133 −0.706 1.00 43.75 C ATOM 2398 O GLN C3076 22.660−19.165 −0.149 1.00 44.83 O ATOM 2399 N ASP C3077 23.070 −17.074 −0.8621.00 43.01 N ATOM 2400 CA ASP C3077 24.442 −17.065 −0.377 1.00 41.11 CATOM 2401 CB ASP C3077 25.315 −16.254 −1.333 1.00 44.24 C ATOM 2402 CGASP C3077 25.261 −16.789 −2.756 1.00 45.88 C ATOM 2403 OD1 ASP C307725.692 −17.943 −2.974 1.00 47.04 O ATOM 2404 OD2 ASP C3077 24.777−16.064 −3.652 1.00 46.86 O ATOM 2405 C ASP C3077 24.493 −16.481 1.0281.00 38.51 C ATOM 2406 O ASP C3077 25.564 −16.291 1.598 1.00 39.35 OATOM 2407 N LEU C3078 23.319 −16.194 1.578 1.00 35.03 N ATOM 2408 CA LEUC3078 23.199 −15.649 2.927 1.00 31.01 C ATOM 2409 CB LEU C3078 22.479−14.296 2.889 1.00 30.66 C ATOM 2410 CG LEU C3078 23.280 −13.026 2.5841.00 31.31 C ATOM 2411 CD1 LEU C3078 24.253 −13.251 1.440 1.00 33.52 CATOM 2412 CD2 LEU C3078 22.303 −11.900 2.254 1.00 30.14 C ATOM 2413 CLEU C3078 22.396 −16.632 3.778 1.00 28.65 C ATOM 2414 O LEU C3078 21.391−17.178 3.322 1.00 28.16 O ATOM 2415 N GLU C3079 22.839 −16.860 5.0091.00 25.38 N ATOM 2416 CA GLU C3079 22.138 −17.779 5.895 1.00 24.35 CATOM 2417 CB GLU C3079 22.794 −19.163 5.869 1.00 24.49 C ATOM 2418 CGGLU C3079 21.999 −20.224 6.616 1.00 24.73 C ATOM 2419 CD GLU C307922.653 −21.592 6.558 1.00 26.90 C ATOM 2420 OE1 GLU C3079 23.770 −21.7407.089 1.00 28.68 O ATOM 2421 OE2 GLU C3079 22.053 −22.523 5.979 1.0029.27 O ATOM 2422 C GLU C3079 22.098 −17.267 7.327 1.00 22.68 C ATOM2423 O GLU C3079 23.123 −16.873 7.883 1.00 22.88 O ATOM 2424 N VAL C308020.901 −17.275 7.907 1.00 21.79 N ATOM 2425 CA VAL C3080 20.678 −16.8249.276 1.00 21.18 C ATOM 2426 CB VAL C3080 19.705 −15.621 9.325 1.0022.20 C ATOM 2427 CG1 VAL C3080 19.404 −15.244 10.777 1.00 20.66 C ATOM2428 CG2 VAL C3080 20.311 −14.435 8.587 1.00 23.11 C ATOM 2429 C VALC3080 20.064 −17.971 10.060 1.00 20.45 C ATOM 2430 O VAL C3080 18.972−18.429 9.743 1.00 19.50 O ATOM 2431 N LEU C3081 20.781 −18.441 11.0721.00 20.00 N ATOM 2432 CA LEU C3081 20.303 −19.540 11.897 1.00 21.15 CATOM 2433 CB LEU C3081 21.328 −20.686 11.905 1.00 21.34 C ATOM 2434 CGLEU C3081 21.677 −21.275 10.528 1.00 22.27 C ATOM 2435 CD1 LEU C308122.713 −22.396 10.653 1.00 23.04 C ATOM 2436 CD2 LEU C3081 20.400−21.802 9.884 1.00 24.47 C ATOM 2437 C LEU C3081 20.107 −19.003 13.3001.00 21.01 C ATOM 2438 O LEU C3081 20.287 −17.811 13.541 1.00 20.54 OATOM 2439 N ASN C3082 19.732 −19.881 14.220 1.00 21.50 N ATOM 2440 CAASN C3082 19.530 −19.494 15.608 1.00 22.77 C ATOM 2441 CB ASN C308218.089 −19.783 16.020 1.00 23.53 C ATOM 2442 CG ASN C3082 17.099 −18.88015.310 1.00 25.44 C ATOM 2443 OD1 ASN C3082 16.907 −17.731 15.698 1.0025.60 O ATOM 2444 ND2 ASN C3082 16.488 −19.388 14.247 1.00 27.37 N ATOM2445 C ASN C3082 20.499 −20.258 16.499 1.00 22.68 C ATOM 2446 O ASNC3082 20.629 −21.478 16.380 1.00 21.84 O ATOM 2447 N ASN C3083 21.191−19.541 17.382 1.00 23.99 N ATOM 2448 CA ASN C3083 22.137 −20.187 18.2821.00 23.34 C ATOM 2449 CB ASN C3083 23.141 −19.170 18.840 1.00 24.83 CATOM 2450 CG ASN C3083 22.474 −18.019 19.575 1.00 25.31 C ATOM 2451 OD1ASN C3083 21.405 −18.175 20.174 1.00 23.71 O ATOM 2452 ND2 ASN C308323.116 −16.859 19.550 1.00 26.83 N ATOM 2453 C ASN C3083 21.381 −20.87719.415 1.00 25.05 C ATOM 2454 O ASN C3083 20.152 −20.876 19.432 1.0022.22 O ATOM 2455 N GLU C3084 22.108 −21.460 20.365 1.00 27.04 N ATOM2456 CA GLU C3084 21.472 −22.174 21.466 1.00 29.78 C ATOM 2457 CB GLUC3084 22.517 −22.954 22.275 1.00 32.58 C ATOM 2458 CG GLU C3084 23.715−22.141 22.711 1.00 36.99 C ATOM 2459 CD GLU C3084 24.857 −22.184 21.7071.00 41.57 C ATOM 2460 OE1 GLU C3084 24.647 −21.812 20.529 1.00 42.03 OATOM 2461 OE2 GLU C3084 25.972 −22.590 22.107 1.00 43.80 O ATOM 2462 CGLU C3084 20.638 −21.294 22.396 1.00 30.13 C ATOM 2463 O GLU C308419.766 −21.796 23.111 1.00 30.37 O ATOM 2464 N ARG C3085 20.901 −19.99122.401 1.00 28.98 N ATOM 2465 CA ARG C3085 20.119 −19.088 23.238 1.0030.28 C ATOM 2466 CB ARG C3085 20.976 −17.912 23.716 1.00 31.17 C ATOM2467 CG ARG C3085 22.055 −18.340 24.705 1.00 34.80 C ATOM 2468 CD ARGC3085 23.056 −17.237 24.995 1.00 37.35 C ATOM 2469 NE ARG C3085 24.367−17.801 25.310 1.00 40.35 N ATOM 2470 CZ ARG C3085 24.634 −18.518 26.3961.00 40.77 C ATOM 2471 NH1 ARG C3085 23.681 −18.757 27.285 1.00 42.29 NATOM 2472 NH2 ARG C3085 25.852 −19.007 26.587 1.00 41.71 N ATOM 2473 CARG C3085 18.918 −18.597 22.438 1.00 29.32 C ATOM 2474 O ARG C308518.112 −17.806 22.923 1.00 30.16 O ATOM 2475 N GLY C3086 18.805 −19.08621.207 1.00 27.92 N ATOM 2476 CA GLY C3086 17.690 −18.714 20.350 1.0026.11 C ATOM 2477 C GLY C3086 17.893 −17.452 19.530 1.00 25.66 C ATOM2478 O GLY C3086 17.005 −17.044 18.782 1.00 26.33 O ATOM 2479 N ALAC3087 19.061 −16.831 19.654 1.00 23.88 N ATOM 2480 CA ALA C3087 19.328−15.613 18.914 1.00 22.63 C ATOM 2481 CB ALA C3087 20.408 −14.797 19.6101.00 21.67 C ATOM 2482 C ALA C3087 19.742 −15.893 17.478 1.00 22.49 CATOM 2483 O ALA C3087 20.515 −16.808 17.210 1.00 22.63 O ATOM 2484 N PROC3088 19.220 −15.098 16.532 1.00 21.73 N ATOM 2485 CD PRO 03088 18.185−14.068 16.740 1.00 21.19 C ATOM 2486 CA PRO C3088 19.536 −15.244 15.1121.00 20.08 C ATOM 2487 CB PRO C3088 18.434 −14.435 14.435 1.00 22.01 CATOM 2488 CG PRO C3088 18.196 −13.325 15.412 1.00 23.33 C ATOM 2489 CPRO C3088 20.931 −14.689 14.822 1.00 20.77 C ATOM 2490 O PRO C308821.360 −13.704 15.434 1.00 19.53 O ATOM 2491 N TYR C3089 21.647 −15.32713.903 1.00 18.65 N ATOM 2492 CA TYR C3089 22.986 −14.869 13.548 1.0018.94 C ATOM 2493 CB TYR C3089 24.015 −15.410 14.557 1.00 19.72 C ATOM2494 CG TYR C3089 24.295 −16.891 14.434 1.00 20.97 C ATOM 2495 CD1 TYRC3089 25.313 −17.360 13.600 1.00 21.58 C ATOM 2496 CE1 TYR C3089 25.549−18.721 13.448 1.00 21.20 C ATOM 2497 CD2 TYR C3089 23.521 −17.82615.118 1.00 21.44 C ATOM 2498 CE2 TYR C3089 23.748 −19.193 14.974 1.0021.49 C ATOM 2499 CZ TYR C3089 24.764 −19.630 14.133 1.00 20.90 C ATOM2500 OH TYR C3089 24.980 −20.972 13.961 1.00 21.13 O ATOM 2501 C TYRC3089 23.310 −15.356 12.142 1.00 19.33 C ATOM 2502 O TYR C3089 22.695−16.305 11.658 1.00 18.04 O ATOM 2503 N PHE C3090 24.252 −14.694 11.4761.00 21.68 N ATOM 2504 CA PHE C3090 24.644 −15.095 10.129 1.00 22.43 CATOM 2505 CB PHE C3090 25.224 −13.921 9.343 1.00 21.81 C ATOM 2506 CGPHE C3090 24.187 −13.057 8.686 1.00 22.97 C ATOM 2507 CD1 PHE C309023.627 −11.980 9.364 1.00 22.58 C ATOM 2508 CD2 PHE C3090 23.774 −13.3177.382 1.00 22.20 C ATOM 2509 CE1 PHE C3090 22.670 −11.172 8.752 1.0021.60 C ATOM 2510 CE2 PHE C3090 22.815 −12.512 6.762 1.00 21.04 C ATOM2511 CZ PHE C3090 22.267 −11.439 7.453 1.00 20.05 C ATOM 2512 C PHEC3090 25.681 −16.201 10.185 1.00 23.74 C ATOM 2513 O PHE C3090 26.804−15.992 10.642 1.00 23.80 O ATOM 2514 N SER C3091 25.291 −17.381 9.7271.00 25.13 N ATOM 2515 CA SER C3091 26.186 −18.522 9.707 1.00 24.76 CATOM 2516 CB SER C3091 25.378 −19.805 9.790 1.00 25.31 C ATOM 2517 OGSER C3091 24.465 −19.856 8.709 1.00 25.46 O ATOM 2518 C SER C3091 26.959−18.493 8.393 1.00 25.15 C ATOM 2519 O SER C3091 28.036 −19.075 8.2851.00 24.95 O ATOM 2520 N GLN C3092 26.398 −17.806 7.401 1.00 25.28 NATOM 2521 CA GLN C3092 27.012 −17.701 6.079 1.00 26.50 C ATOM 2522 CBGLN C3092 26.414 −18.759 5.150 1.00 29.33 C ATOM 2523 CG GLN C309226.948 −18.723 3.728 1.00 33.15 C ATOM 2524 CD GLN C3092 28.353 −19.2713.638 1.00 35.44 C ATOM 2525 OE1 GLN C3092 29.292 −18.711 4.204 1.0036.58 O ATOM 2526 NE2 GLN C3092 28.503 −20.384 2.935 1.00 37.04 N ATOM2527 C GLN C3092 26.780 −16.323 5.465 1.00 25.49 C ATOM 2528 O GLN C309225.637 −15.871 5.365 1.00 24.76 O ATOM 2529 N ALA C3093 27.864 −15.6745.042 1.00 24.56 N ATOM 2530 CA ALA C3093 27.801 −14.350 4.422 1.0024.82 C ATOM 2531 CB ALA C3093 27.400 −13.302 5.451 1.00 24.36 C ATOM2532 C ALA C3093 29.152 −13.978 3.808 1.00 24.47 C ATOM 2533 O ALA C309330.200 −14.284 4.365 1.00 24.58 O ATOM 2534 N PRO C3094 29.137 −13.2892.654 1.00 25.93 N ATOM 2535 CD PRO C3094 27.920 −12.815 1.965 1.0024.23 C ATOM 2536 CA PRO C3094 30.345 −12.860 1.935 1.00 25.56 C ATOM2537 CB PRO C3094 29.788 −12.404 0.592 1.00 26.20 C ATOM 2538 CG PROC3094 28.472 −11.792 0.997 1.00 26.19 C ATOM 2539 C PRO C3094 31.098−11.744 2.658 1.00 26.12 C ATOM 2540 O PRO C3094 31.403 −10.703 2.0771.00 25.63 O ATOM 2541 N PHE C3095 31.404 −11.971 3.930 1.00 26.90 NATOM 2542 CA PHE C3095 32.098 −10.977 4.739 1.00 26.88 C ATOM 2543 CBPHE C3095 31.068 −10.004 5.331 1.00 26.61 C ATOM 2544 CG PHE C309531.665 −8.923 6.179 1.00 26.50 C ATOM 2545 CD1 PHE C3095 31.491 −8.9317.559 1.00 25.34 C ATOM 2546 CD2 PHE C3095 32.406 −7.895 5.601 1.0026.22 C ATOM 2547 CE1 PHE C3095 32.043 −7.937 8.350 1.00 24.07 C ATOM2548 CE2 PHE C3095 32.964 −6.895 6.384 1.00 25.18 C ATOM 2549 CZ PHEC3095 32.781 −6.917 7.764 1.00 26.71 C ATOM 2550 C PHE C3095 32.830−11.726 5.841 1.00 27.07 C ATOM 2551 O PHE C3095 32.234 −12.547 6.5271.00 28.82 O ATOM 2552 N SER C3096 34.119 −11.450 6.013 1.00 27.08 NATOM 2553 CA SER C3096 34.907 −12.153 7.022 1.00 26.87 C ATOM 2554 CBSER C3096 36.287 −12.488 6.457 1.00 27.85 C ATOM 2555 OG SER C309636.967 −11.315 6.073 1.00 29.01 O ATOM 2556 C SER C3096 35.072 −11.4468.364 1.00 27.60 C ATOM 2557 O SER C3096 35.753 −11.957 9.251 1.00 28.27O ATOM 2558 N GLY C3097 34.466 −10.271 8.513 1.00 26.02 N ATOM 2559 CAGLY C3097 34.559 −9.558 9.775 1.00 25.74 C ATOM 2560 C GLY C3097 33.406−9.991 10.664 1.00 26.75 C ATOM 2561 O GLY C3097 32.796 −11.029 10.4221.00 26.07 O ATOM 2562 N LYS C3098 33.084 −9.202 11.682 1.00 25.99 NATOM 2563 CA LYS C3098 31.985 −9.559 12.572 1.00 26.80 C ATOM 2564 CBLYS C3098 32.302 −9.106 13.998 1.00 28.83 C ATOM 2565 CG LYS C309833.742 −9.410 14.383 1.00 33.82 C ATOM 2566 CD LYS C3098 34.014 −9.22715.860 1.00 37.34 C ATOM 2567 CE LYS C3098 33.574 −10.444 16.652 1.0039.78 C ATOM 2568 NZ LYS C3098 33.986 −10.326 18.084 1.00 40.81 N ATOM2569 C LYS C3098 30.676 −8.944 12.095 1.00 25.06 C ATOM 2570 O LYS C309830.633 −7.785 11.670 1.00 24.85 O ATOM 2571 N ILE C3099 29.611 −9.73712.152 1.00 22.88 N ATOM 2572 CA ILE C3099 28.292 −9.286 11.730 1.0020.01 C ATOM 2573 CB ILE C3099 27.688 −10.246 10.687 1.00 19.89 C ATOM2574 CG2 ILE C3099 26.373 −9.674 10.150 1.00 15.87 C ATOM 2575 CG1 ILEC3099 28.686 −10.474 9.548 1.00 18.98 C ATOM 2576 CD1 ILE C3099 28.241−11.543 8.561 1.00 19.71 C ATOM 2577 C ILE C3099 27.364 −9.243 12.9411.00 20.05 C ATOM 2578 O ILE C3099 26.967 −10.289 13.459 1.00 21.97 OATOM 2579 N TRP C3100 27.032 −8.038 13.398 1.00 18.21 N ATOM 2580 CA TRPC3100 26.140 −7.880 14.541 1.00 17.20 C ATOM 2581 CB TRP C3100 26.570−6.678 15.383 1.00 17.48 C ATOM 2582 CG TRP C3100 27.959 −6.851 15.9481.00 17.00 C ATOM 2583 CD2 TRP C3100 28.323 −7.642 17.085 1.00 16.80 CATOM 2584 CE2 TRP C3100 29.724 −7.538 17.237 1.00 18.05 C ATOM 2585 CE3TRP C3100 27.599 −8.431 17.992 1.00 19.31 C ATOM 2586 CD1 TRP C310029.119 −6.316 15.465 1.00 17.86 C ATOM 2587 NE1 TRP C3100 30.188 −6.72416.236 1.00 18.87 N ATOM 2588 CZ2 TRP C3100 30.417 −8.192 18.263 1.0019.19 C ATOM 2589 CZ3 TRP C3100 28.290 −9.082 19.012 1.00 19.20 C ATOM2590 CH2 TRP C3100 29.687 −8.955 19.136 1.00 17.94 C ATOM 2591 C TRPC3100 24.717 −7.699 14.018 1.00 17.56 C ATOM 2592 O TRP C3100 24.365−6.656 13.461 1.00 18.14 O ATOM 2593 N LEU C3101 23.916 −8.742 14.1911.00 17.00 N ATOM 2594 CA LEU C3101 22.540 −8.764 13.725 1.00 16.11 CATOM 2595 CB LEU C3101 22.321 −9.991 12.837 1.00 16.56 C ATOM 2596 CGLEU C3101 20.875 −10.417 12.559 1.00 16.77 C ATOM 2597 CD1 LEU C310120.194 −9.413 11.625 1.00 15.60 C ATOM 2598 CD2 LEU C3101 20.883 −11.80911.939 1.00 18.41 C ATOM 2599 C LEU C3101 21.525 −8.811 14.852 1.0016.81 C ATOM 2600 O LEU C3101 21.746 −9.435 15.890 1.00 14.02 O ATOM2601 N SER C3102 20.410 −8.128 14.638 1.00 15.53 N ATOM 2602 CA SERC3102 19.316 −8.151 15.588 1.00 14.91 C ATOM 2603 CB SER C3102 19.424−7.035 16.619 1.00 14.40 C ATOM 2604 OG SER C3102 18.483 −7.263 17.6571.00 15.41 O ATOM 2605 C SER C3102 18.052 −7.981 14.761 1.00 14.92 CATOM 2606 O SER C3102 18.020 −7.195 13.805 1.00 14.51 O ATOM 2607 N ILEC3103 17.023 −8.734 15.129 1.00 14.41 N ATOM 2608 CA ILE C3103 15.744−8.710 14.437 1.00 15.86 C ATOM 2609 CB ILE C3103 15.490 −10.043 13.6681.00 16.91 C ATOM 2610 CG2 ILE C3103 14.171 −9.958 12.880 1.00 18.33 CATOM 2611 CG1 ILE C3103 16.665 −10.353 12.737 1.00 18.54 C ATOM 2612 CD1ILE C3103 16.557 −11.729 12.042 1.00 20.00 C ATOM 2613 C ILE C310314.657 −8.608 15.495 1.00 17.43 C ATOM 2614 O ILE C3103 14.805 −9.14816.594 1.00 17.45 O ATOM 2615 N SER C3104 13.566 −7.929 15.157 1.0018.17 N ATOM 2616 CA SER C3104 12.439 −7.798 16.070 1.00 20.57 C ATOM2617 CB SER C3104 12.610 −6.583 16.986 1.00 19.79 C ATOM 2618 OG SERC3104 11.596 −6.571 17.981 1.00 23.17 O ATOM 2619 C SER C3104 11.188−7.645 15.214 1.00 22.21 C ATOM 2620 O SER C3104 11.269 −7.301 14.0331.00 22.47 O ATOM 2621 N HIS C3105 10.028 −7.889 15.796 1.00 23.30 NATOM 2622 CA HIS C3105 8.818 −7.784 15.009 1.00 25.44 C ATOM 2623 CB HISC3105 8.597 −9.083 14.241 1.00 27.72 C ATOM 2624 CG HIS C3105 8.509−10.287 15.125 1.00 29.50 C ATOM 2625 CD2 HIS C3105 7.438 −10.938 15.6391.00 33.02 C ATOM 2626 ND1 HIS C3105 9.622 −10.934 15.615 1.00 32.99 NATOM 2627 CE1 HIS C3105 9.242 −11.933 16.393 1.00 34.27 C ATOM 2628 NE2HIS C3105 7.922 −11.956 16.424 1.00 33.98 N ATOM 2629 C HIS C3105 7.565−7.489 15.805 1.00 26.04 C ATOM 2630 O HIS C3105 7.499 −7.729 17.0091.00 23.14 O ATOM 2631 N THR C3106 6.575 −6.972 15.086 1.00 28.54 N ATOM2632 CA THR C3106 5.261 −6.652 15.613 1.00 30.04 C ATOM 2633 CB THRC3106 4.855 −5.209 15.300 1.00 31.60 C ATOM 2634 OG1 THR C3106 4.804−5.030 13.878 1.00 31.75 O ATOM 2635 CG2 THR C3106 5.848 −4.231 15.9051.00 30.63 C ATOM 2636 C THR C3106 4.332 −7.576 14.840 1.00 30.05 C ATOM2637 O THR C3106 4.792 −8.451 14.101 1.00 31.00 O ATOM 2638 N ASP C31073.031 −7.374 14.987 1.00 31.29 N ATOM 2639 CA ASP C3107 2.056 −8.20614.296 1.00 32.30 C ATOM 2640 CB ASP C3107 0.674 −8.033 14.934 1.0036.82 C ATOM 2641 CG ASP C3107 0.596 −8.612 16.327 1.00 40.78 C ATOM2642 OD1 ASP C3107 −0.205 −8.097 17.136 1.00 44.76 O ATOM 2643 OD2 ASPC3107 1.319 −9.591 16.612 1.00 44.36 O ATOM 2644 C ASP C3107 1.959−7.890 12.807 1.00 31.24 C ATOM 2645 O ASP C3107 1.521 −8.729 12.0261.00 32.84 O ATOM 2646 N GLN C3108 2.374 −6.690 12.410 1.00 28.20 N ATOM2647 CA GLN C3108 2.284 −6.289 11.009 1.00 27.03 C ATOM 2648 CB GLNC3108 1.590 −4.928 10.877 0.05 26.57 C ATOM 2649 CG GLN C3108 0.284−4.788 11.626 0.05 26.25 C ATOM 2650 CD GLN C3108 0.486 −4.733 13.1210.05 26.05 C ATOM 2651 OE1 GLN C3108 1.220 −3.887 13.631 0.05 25.96 OATOM 2652 NE2 GLN C3108 −0.165 −5.636 13.834 0.05 25.84 N ATOM 2653 CGLN C3108 3.607 −6.204 10.264 1.00 25.37 C ATOM 2654 O GLN C3108 3.624−6.210 9.032 1.00 24.85 O ATOM 2655 N PHE C3109 4.716 −6.098 10.987 1.0024.20 N ATOM 2656 CA PHE C3109 5.996 −5.994 10.299 1.00 23.19 C ATOM2657 CB PHE C3109 6.210 −4.548 9.827 1.00 24.65 C ATOM 2658 CG PHE C31096.268 −3.541 10.947 1.00 26.19 C ATOM 2659 CD1 PHE C3109 7.406 −3.42111.738 1.00 26.36 C ATOM 2660 CD2 PHE C3109 5.181 −2.714 11.211 1.0027.63 C ATOM 2661 CE1 PHE C3109 7.464 −2.490 12.780 1.00 26.39 C ATOM2662 CE2 PHE C3109 5.225 −1.780 12.249 1.00 28.63 C ATOM 2663 CZ PHEC3109 6.371 −1.669 13.036 1.00 28.60 C ATOM 2664 C PHE C3109 7.191−6.459 11.116 1.00 21.14 C ATOM 2665 O PHE C3109 7.100 −6.648 12.3281.00 19.22 O ATOM 2666 N VAL C3110 8.308 −6.650 10.425 1.00 19.26 N ATOM2667 CA VAL C3110 9.550 −7.083 11.052 1.00 19.85 C ATOM 2668 CB VALC3110 10.027 −8.438 10.471 1.00 21.25 C ATOM 2669 CG1 VAL C3110 11.360−8.859 11.101 1.00 23.25 C ATOM 2670 CG2 VAL C3110 8.980 −9.488 10.7191.00 25.17 C ATOM 2671 C VAL C3110 10.604 −6.039 10.737 1.00 19.21 CATOM 2672 O VAL C3110 10.503 −5.345 9.725 1.00 19.53 O ATOM 2673 N THRC3111 11.603 −5.925 11.608 1.00 19.09 N ATOM 2674 CA THR C3111 12.695−4.984 11.409 1.00 20.72 C ATOM 2675 CB THR C3111 12.608 −3.765 12.3681.00 22.75 C ATOM 2676 OG1 THR C3111 12.635 −4.216 13.730 1.00 26.03 OATOM 2677 CG2 THR C3111 11.322 −2.976 12.124 1.00 22.96 C ATOM 2678 CTHR C3111 13.993 −5.725 11.684 1.00 20.16 C ATOM 2679 O THR C3111 14.024−6.664 12.481 1.00 20.27 O ATOM 2680 N ALA C3112 15.060 −5.312 11.0101.00 19.72 N ATOM 2681 CA ALA C3112 16.361 −5.935 11.201 1.00 19.77 CATOM 2682 CB ALA C3112 16.617 −6.975 10.109 1.00 18.61 C ATOM 2683 C ALAC3112 17.441 −4.868 11.172 1.00 19.41 C ATOM 2684 O ALA C3112 17.337−3.885 10.442 1.00 22.32 O ATOM 2685 N SER C3113 18.474 −5.062 11.9801.00 20.21 N ATOM 2686 CA SER C3113 19.579 −4.124 12.045 1.00 18.53 CATOM 2687 CB SER C3113 19.506 −3.298 13.327 1.00 19.50 C ATOM 2688 OGSER C3113 20.510 −2.293 13.328 1.00 19.90 O ATOM 2689 C SER C3113 20.888−4.895 12.003 1.00 18.71 C ATOM 2690 O SER C3113 21.084 −5.843 12.7671.00 16.55 O ATOM 2691 N VAL C3114 21.779 −4.472 11.107 1.00 17.09 NATOM 2692 CA VAL C3114 23.071 −5.115 10.930 1.00 17.37 C ATOM 2693 CBVAL C3114 23.145 −5.842 9.563 1.00 16.61 C ATOM 2694 CG1 VAL C311424.593 −6.263 9.255 1.00 18.34 C ATOM 2695 CG2 VAL C3114 22.244 −7.0509.576 1.00 16.94 C ATOM 2696 C VAL C3114 24.216 −4.116 10.993 1.00 16.94C ATOM 2697 O VAL C3114 24.145 −3.043 10.408 1.00 16.28 O ATOM 2698 NILE C3115 25.265 −4.477 11.720 1.00 17.86 N ATOM 2699 CA ILE C311526.446 −3.632 11.820 1.00 19.21 C ATOM 2700 CB ILE C3115 26.667 −3.08513.253 1.00 19.71 C ATOM 2701 CG2 ILE C3115 27.926 −2.217 13.287 1.0019.20 C ATOM 2702 CG1 ILE C3115 25.451 −2.268 13.703 1.00 19.12 C ATOM2703 CD1 ILE C3115 25.573 −1.701 15.110 1.00 20.38 C ATOM 2704 C ILEC3115 27.627 −4.516 11.440 1.00 18.95 C ATOM 2705 O ILE C3115 27.806−5.589 12.007 1.00 18.31 O ATOM 2706 N LEU C3116 28.409 −4.076 10.4571.00 19.22 N ATOM 2707 CA LEU C3116 29.578 −4.830 10.021 1.00 20.77 CATOM 2708 CB LEU C3116 29.696 −4.805 8.493 1.00 20.70 C ATOM 2709 CG LEUC3116 28.445 −5.235 7.703 1.00 19.25 C ATOM 2710 CD1 LEU C3116 28.758−5.249 6.218 1.00 21.02 C ATOM 2711 CD2 LEU C3116 27.996 −6.614 8.1501.00 19.48 C ATOM 2712 C LEU C3116 30.803 −4.182 10.655 1.00 21.44 CATOM 2713 O LEU C3116 30.996 −2.969 10.554 1.00 21.12 O ATOM 2714 N GLUC3117 31.620 −4.994 11.314 1.00 23.48 N ATOM 2715 CA GLU C3117 32.812−4.493 11.987 1.00 26.83 C ATOM 2716 CB GLU C3117 32.571 −4.457 13.5041.00 27.48 C ATOM 2717 CG GLU C3117 33.817 −4.166 14.343 1.00 30.16 CATOM 2718 CD GLU C3117 33.628 −4.470 15.826 1.00 29.66 C ATOM 2719 OE1GLU C3117 33.182 −5.595 16.158 1.00 29.18 O ATOM 2720 OE2 GLU C311733.932 −3.585 16.660 1.00 29.22 O ATOM 2721 C GLU C3117 34.048 −5.33511.680 1.00 28.97 C ATOM 2722 O GLU C3117 33.978 −6.563 11.578 1.0027.81 O ATOM 2723 N GLU C3118 35.178 −4.657 11.513 1.00 31.18 N ATOM2724 CA GLU C3118 36.446 −5.323 11.248 1.00 35.42 C ATOM 2725 CB GLUC3118 37.015 −4.880 9.893 1.00 37.41 C ATOM 2726 CG GLU C3118 36.592−5.772 8.727 1.00 41.62 C ATOM 2727 CD GLU C3118 37.041 −5.248 7.3681.00 43.91 C ATOM 2728 OE1 GLU C3118 38.193 −4.776 7.253 1.00 46.07 OATOM 2729 OE2 GLU C3118 36.242 −5.321 6.409 1.00 44.10 O ATOM 2730 C GLUC3118 37.414 −4.963 12.369 1.00 35.74 C ATOM 2731 O GLU C3118 37.417−3.784 12.785 1.00 35.88 O ATOM 2732 OXT GLU C3118 38.154 −5.858 12.8211.00 38.35 O TER 2733 GLU C3118 ATOM 2734 O HOH W4002 24.915 17.15436.149 1.00 24.34 O ATOM 2735 O HOH W4003 1.430 5.412 7.521 1.00 22.65 OATOM 2736 O HOH W4004 15.230 −11.883 17.512 1.00 29.62 O ATOM 2737 O HOHW4006 20.551 4.946 39.709 1.00 33.21 O ATOM 2738 O HOH W4008 0.49712.883 37.515 1.00 46.32 O ATOM 2739 O HOH W4009 22.219 1.070 4.722 1.0020.90 O ATOM 2740 O HOH W4010 23.057 4.216 27.783 1.00 22.10 O ATOM 2741O HOH W4012 26.158 9.664 6.047 1.00 26.69 O ATOM 2742 O HOH W4013 13.195−14.652 11.137 1.00 18.24 O ATOM 2743 O HOH W4014 32.126 −19.177 9.5621.00 41.78 O ATOM 2744 O HOH W4016 11.365 8.055 −2.295 1.00 29.34 O ATOM2745 O HOH W4017 16.979 7.951 22.041 1.00 23.20 O ATOM 2746 O HOH W401820.734 17.150 36.413 1.00 25.86 O ATOM 2747 O HOH W4020 −9.281 −6.38741.928 1.00 31.95 O ATOM 2748 O HOH W4021 18.869 −12.662 22.632 1.0030.51 O ATOM 2749 O HOH W4025 18.802 13.286 −2.320 1.00 31.86 O ATOM2750 O HOH W4026 26.500 16.583 31.811 1.00 52.21 O ATOM 2751 O HOH W40276.858 −4.124 3.265 1.00 23.26 O ATOM 2752 O HOH W4028 10.702 1.088−3.405 1.00 41.81 O ATOM 2753 O HOH W4029 12.811 8.598 27.541 1.00 33.12O ATOM 2754 O HOH W4031 12.749 −8.445 19.973 1.00 24.85 O ATOM 2755 OHOH W4032 13.535 0.610 2.032 1.00 40.39 O ATOM 2756 O HOH W4033 13.5948.162 33.675 1.00 30.23 O ATOM 2757 O HOH W4035 10.527 5.028 27.661 1.0022.20 O ATOM 2758 O HOH W4038 10.071 6.775 24.507 1.00 34.64 O ATOM 2759O HOH W4039 22.581 2.348 2.717 1.00 30.28 O ATOM 2760 O HOH W4041 34.765−18.840 6.665 1.00 52.31 O ATOM 2761 O HOH W4042 19.832 10.430 22.3621.00 30.27 O ATOM 2762 O HOH W4043 25.556 −0.749 36.545 1.00 47.38 OATOM 2763 O HOH W4044 1.280 −1.711 37.119 1.00 35.25 O ATOM 2764 O HOHW4045 23.055 −3.951 37.102 1.00 29.32 O ATOM 2765 O HOH W4046 10.3469.220 18.446 1.00 31.53 O ATOM 2766 O HOH W4047 −3.287 0.403 31.271 1.0053.94 O ATOM 2767 O HOH W4048 4.921 −2.235 2.298 1.00 35.71 O ATOM 2768O HOH W4050 4.512 −5.663 22.584 1.00 34.27 O ATOM 2769 O HOH W405132.165 −16.448 3.541 1.00 29.46 O ATOM 2770 O HOH W4052 17.356 −10.55417.298 1.00 20.37 O ATOM 2771 O HOH W4053 23.079 8.307 36.567 1.00 27.23O ATOM 2772 O HOH W4054 22.333 9.961 24.703 1.00 41.93 O ATOM 2773 O HOHW4055 19.848 3.106 3.638 1.00 23.68 O ATOM 2774 O HOH W4056 14.228 9.5472.164 1.00 13.78 O ATOM 2775 O HOH W4057 −5.992 9.409 37.088 1.00 40.47O ATOM 2776 O HOH W4058 15.141 2.885 1.432 1.00 32.54 O ATOM 2777 O HOHW4059 27.207 3.715 −0.205 1.00 38.02 O ATOM 2778 O HOH W4060 4.520 8.61713.683 1.00 29.66 O ATOM 2779 O HOH W4061 −0.534 22.844 0.843 1.00 43.95O ATOM 2780 O HOH W4062 33.271 0.399 4.561 1.00 41.51 O ATOM 2781 O HOHW4063 10.750 −9.990 18.523 1.00 37.79 O ATOM 2782 O HOH W4065 35.0032.841 10.072 1.00 34.95 O ATOM 2783 O HOH W4066 15.619 13.987 20.0591.00 51.87 O ATOM 2784 O HOH W4067 30.322 −16.861 5.985 1.00 25.67 OATOM 2785 O HOH W4068 −3.928 16.855 6.776 1.00 37.28 O ATOM 2786 O HOHW4069 20.489 9.067 39.451 1.00 48.83 O ATOM 2787 O HOH W4070 38.865−2.991 24.079 1.00 52.94 O ATOM 2788 O HOH W4071 18.289 12.534 22.2751.00 32.83 O ATOM 2789 O HOH W4072 16.738 0.024 14.519 1.00 34.01 O ATOM2790 O HOH W4073 1.959 −19.500 14.371 1.00 40.61 O ATOM 2791 O HOH W40741.805 −19.989 7.096 1.00 40.73 O ATOM 2792 O HOH W4075 15.612 10.43434.742 1.00 32.10 O ATOM 2793 O HOH W4076 13.088 0.232 13.391 1.00 37.71O ATOM 2794 O HOH W4077 −3.125 13.706 3.280 1.00 34.62 O ATOM 2795 O HOHW4078 2.257 8.002 15.256 1.00 30.49 O ATOM 2796 O HOH W4079 1.805 3.82014.707 1.00 34.86 O ATOM 2797 O HOH W4080 5.391 −8.908 −2.363 1.00 35.80O ATOM 2798 O HOH W4081 13.173 18.130 19.444 1.00 42.58 O ATOM 2799 OHOH W4083 3.428 25.760 7.166 1.00 47.46 O ATOM 2800 O HOH W4085 19.6000.144 14.509 1.00 27.27 O ATOM 2801 O HOH W4086 17.905 −21.379 25.3521.00 38.73 O ATOM 2802 O HOH W4087 33.360 5.719 22.662 1.00 36.03 O ATOM2803 O HOH W4089 9.617 −0.859 41.147 1.00 32.45 O ATOM 2804 O HOH W409028.109 −16.115 0.982 1.00 29.92 O ATOM 2805 O HOH W4091 38.387 −10.8969.764 1.00 47.94 O ATOM 2806 O HOH W4092 5.988 24.794 8.424 1.00 43.14 OATOM 2807 O HOH W4093 −3.277 6.265 6.376 1.00 35.40 O ATOM 2808 O HOHW4094 30.455 10.041 6.941 1.00 32.99 O ATOM 2809 O HOH W4095 26.8150.664 4.954 1.00 27.85 O ATOM 2810 O HOH W4096 15.273 23.735 −4.277 1.0047.73 O ATOM 2811 O HOH W4099 26.449 1.509 2.656 1.00 65.15 O ATOM 2812O HOH W4100 0.838 7.963 3.230 1.00 37.27 O ATOM 2813 O HOH W4101 29.3818.723 0.899 1.00 43.02 O ATOM 2814 O HOH W4102 40.660 −5.785 23.570 1.0045.63 O ATOM 2815 O HOH W4103 26.328 6.312 5.240 1.00 53.46 O ATOM 2816O HOH W4104 34.720 1.902 16.155 1.00 43.82 O ATOM 2817 O HOH W4105−7.319 −8.388 40.539 1.00 39.00 O ATOM 2818 O HOH W4106 18.869 25.1161.680 1.00 46.38 O ATOM 2819 O HOH W4107 16.340 14.706 24.191 1.00 38.04O ATOM 2820 O HOH W4108 6.923 8.908 27.885 1.00 36.28 O ATOM 2821 O HOHW4109 12.525 −11.624 17.355 1.00 34.51 O ATOM 2822 O HOH W4110 34.314−7.049 18.369 1.00 34.61 O ATOM 2823 O HOH W4113 38.750 −2.512 27.1671.00 57.88 O ATOM 2824 O HOH W4114 18.115 3.750 1.319 1.00 31.45 O ATOM2825 O HOH W4115 27.875 1.248 31.553 1.00 55.12 O ATOM 2826 O HOH W41167.683 −21.130 −8.639 1.00 46.38 O ATOM 2827 O HOH W4117 −0.188 6.86139.329 1.00 45.23 O ATOM 2828 O HOH W4118 15.597 2.256 13.150 1.00 38.63O ATOM 2829 O HOH W4120 29.648 18.094 28.167 1.00 35.93 O ATOM 2830 OHOH W4121 16.930 −20.733 11.766 1.00 37.44 O ATOM 2831 O HOH W4122 7.167−12.636 −7.617 1.00 48.07 O ATOM 2832 O HOH W4123 37.628 10.036 12.6401.00 43.48 O ATOM 2833 O HOH W4124 13.082 −13.269 27.306 1.00 52.38 OATOM 2834 O HOH W4125 4.976 −26.696 6.493 1.00 47.37 O ATOM 2835 O HOHW4126 2.241 −22.225 15.163 1.00 51.68 O ATOM 2836 O HOH W4127 8.988−10.057 20.455 1.00 50.47 O ATOM 2837 O HOH W4128 18.719 −13.639 −6.6161.00 49.20 O ATOM 2838 O HOH W4129 21.651 22.882 0.638 1.00 46.89 O ATOM2839 O HOH W4130 27.239 3.345 29.234 1.00 25.74 O ATOM 2840 O HOH W41319.016 −8.748 −1.209 1.00 45.62 O ATOM 2841 O HOH W4132 13.082 −9.63237.155 1.00 43.55 O ATOM 2842 O HOH W4133 29.378 15.689 6.467 1.00 49.72O ATOM 2843 O HOH W4134 −7.908 −3.988 42.818 1.00 30.81 O ATOM 2844 OHOH W4135 3.562 −8.297 27.665 1.00 45.56 O ATOM 2845 O HOH W4136 −7.199−0.161 28.514 1.00 24.59 O ATOM 2846 O HOH W4137 31.194 6.207 6.288 1.0042.31 O ATOM 2847 O HOH W4138 19.383 8.002 23.933 1.00 35.57 O ATOM 2848O HOH W4139 −6.335 −8.439 24.417 1.00 47.50 O ATOM 2849 O HOH W414037.800 −1.901 17.636 1.00 38.42 O ATOM 2850 O HOH W4141 36.896 4.27913.213 1.00 44.41 O ATOM 2851 O HOH W4142 18.980 16.923 −5.091 1.0032.40 O ATOM 2852 O HOH W4143 6.338 17.886 −7.468 1.00 44.66 O ATOM 2853O HOH W4144 8.099 9.789 −8.452 1.00 34.29 O ATOM 2854 O HOH W4145 22.40022.185 4.929 1.00 58.51 O ATOM 2855 O HOH W4146 23.417 1.724 −2.662 1.0049.61 O ATOM 2856 O HOH W4147 28.353 11.186 5.638 1.00 36.80 O ATOM 2857O HOH W4148 0.018 1.428 9.817 1.00 46.52 O ATOM 2858 O HOH W4149 38.727−0.038 26.083 1.00 50.08 O ATOM 2859 O HOH W4150 24.171 −8.880 20.1791.00 43.36 O ATOM 2860 O HOH W4151 −0.768 −7.980 41.105 1.00 48.48 OATOM 2861 O HOH W4152 26.257 5.046 35.426 1.00 48.00 O ATOM 2862 O HOHW4153 35.432 0.075 28.104 1.00 43.89 O ATOM 2863 O HOH W4154 35.3012.870 27.050 1.00 52.24 O ATOM 2864 O HOH W4155 −4.097 3.796 17.913 1.0044.40 O ATOM 2865 O HOH W4156 29.195 0.822 3.786 1.00 40.55 O ATOM 2866O HOH W4157 15.774 −2.195 11.976 1.00 39.79 O ATOM 2867 O HOH W415822.736 4.680 3.551 1.00 24.63 O ATOM 2868 O HOH W4159 10.086 −24.03817.929 1.00 54.44 O ATOM 2869 O HOH W4161 37.774 −8.164 11.579 1.0059.16 O ATOM 2870 O HOH W4162 25.882 18.452 33.331 1.00 33.59 O ATOM2871 O HOH W4163 −0.430 0.356 12.041 1.00 45.32 O ATOM 2872 O HOH W4164−3.073 −7.128 24.073 1.00 45.12 O ATOM 2873 O HOH W4165 31.655 13.8158.848 1.00 29.05 O ATOM 2874 O HOH W4166 17.133 8.014 −0.782 1.00 24.81O ATOM 2875 O HOH W4167 11.582 −12.517 13.880 1.00 37.19 O ATOM 2876 OHOH W4168 15.057 −15.827 14.902 1.00 25.73 O ATOM 2877 O HOH W416912.130 −17.876 15.236 1.00 35.36 O ATOM 2878 O HOH W4170 7.663 8.07546.234 1.00 31.45 O ATOM 2879 O HOH W4171 8.858 17.412 12.301 1.00 37.47O TER 2880 HOH W4171 END

[0363] TABLE 5 REMARK coordinates from restrained individual B-factorrefinement REMARK refinement resolution: 500.0 − 1.90 A REMARK startingr = 0.2427 free_r = 0.2720 REMARK final r = 0.2425 free_r = 0.2731REMARK B rmsd for bonded mainchain atoms = 0.960  target = 1.5 REMARK Brmsd for bonded sidechain atoms = 1.085  target = 2.0 REMARK B rmsd forangle mainchain atoms = 1.688  target = 2.0 REMARK B rmsd for anglesidechain atoms = 1.768  target = 2.5 REMARK wa = 1.18715 REMARK rweight= 0.298329 REMARK target = mlf steps = 30 REMARK sg = C2  a = 120.188  b= 62.273  c = 51.673  alpha = 90 beta = 98.745  gamma = 90 REMARKparameter file 1  CNX_TOPPAR:protein_rep.param REMARK parameter file2  CNX_TOPPAR:water_rep.param REMARK parameter file3  CNX_TOPPAR:ion.param REMARK parameter file 4  35-ADP/35-ADP.paramREMARK molecular structure file: generate.psf REMARK input coordinates:minimize.pdb REMARK reflection file = ../data/x-ray_data.cv REMARK ncs =none REMARK B-correction resolution: 6.0 − 1.90 REMARK initial B-factorcorrection applied to fobs: REMARK  B11 = 0.036  B22 = −2.635  B33 =2.599 REMARK  B12 = 0.000  B13 = 0.515  B23 = 0.000 REMARK B-factorcorrection applied to coordinate array B: 0.030 REMARK bulk solvent:(Mask) density level = 0.369861 e/A{circumflex over ( )}3, B-factor =96.7512 A{circumflex over ( )}2 REMARK reflections with |Fobs|/sigma_F <0.0 rejected REMARK reflections with |Fobs| > 10000 * rms (Fobs)rejected REMARK theoretical total number of refl. in resol. range: 29870(100.0%) REMARK number of unobserved reflections (no entry or |F| = 0):330 (1.1%) REMARK number of reflections rejected: 0 (0.0%) REMARK totalnumber of reflections used: 29540 (98.9%) REMARK number of reflectionsin working set: 28083 (94.0%) REMARK number of reflections in test set:1457 (4.9%) REMARK FILENAME = “acps 35-ADP.pdb” REMARK Written by CNXVERSION: 2000 ATOM 1 CB MET A1003 37.264 5.634 20.230 1.00 26.46 C ATOM2 CG MET A1003 36.648 6.209 21.498 1.00 29.51 C ATOM 3 SD MET A100337.784 7.312 22.398 1.00 33.70 S ATOM 4 CE MET A1003 37.843 8.718 21.2911.00 32.08 C ATOM 5 C MET A1003 35.048 5.262 19.102 1.00 23.04 C ATOM 6O MET A1003 35.009 6.245 18.358 1.00 22.46 O ATOM 7 N MET A1003 37.1084.155 18.256 1.00 24.80 N ATOM 8 CA MET A1003 36.389 4.622 19.479 1.0024.32 C ATOM 9 N ILE A1004 33.957 4.690 19.606 1.00 22.15 N ATOM 10 CAILE A1004 32.606 5.202 19.348 1.00 21.16 C ATOM 11 CB ILE A1004 31.5354.120 19.670 1.00 21.51 C ATOM 12 CG2 ILE A1004 30.122 4.710 19.558 1.0021.66 C ATOM 13 CG1 ILE A1004 31.696 2.927 18.722 1.00 21.75 C ATOM 14CD1 ILE A1004 30.823 1.734 19.074 1.00 22.20 C ATOM 15 C ILE A100432.361 6.417 20.245 1.00 20.57 C ATOM 16 O ILE A1004 32.773 6.416 21.4071.00 21.36 O ATOM 17 N VAL A1005 31.705 7.448 19.713 1.00 19.47 N ATOM18 CA VAL A1005 31.409 8.652 20.492 1.00 18.73 C ATOM 19 CB VAL A100532.308 9.852 20.042 1.00 19.66 C ATOM 20 CG1 VAL A1005 33.779 9.53020.319 1.00 20.39 C ATOM 21 CG2 VAL A1005 32.119 10.142 18.562 1.0020.39 C ATOM 22 C VAL A1005 29.924 9.085 20.502 1.00 17.55 C ATOM 23 OVAL A1005 29.601 10.193 20.940 1.00 16.98 O ATOM 24 N GLY A1006 29.0268.207 20.041 1.00 16.14 N ATOM 25 CA GLY A1006 27.593 8.513 20.046 1.0014.83 C ATOM 26 C GLY A1006 26.725 7.566 19.216 1.00 13.78 C ATOM 27 OGLY A1006 27.223 6.982 18.257 1.00 12.47 O ATOM 28 N HIS A1007 25.4427.409 19.581 1.00 13.88 N ATOM 29 CA HIS A1007 24.495 6.535 18.844 1.0014.19 C ATOM 30 CB HIS A1007 24.638 5.080 19.332 1.00 14.36 C ATOM 31 CGHIS A1007 23.663 4.115 18.711 1.00 14.94 C ATOM 32 CD2 HIS A1007 22.9043.137 19.266 1.00 15.52 C ATOM 33 ND1 HIS A1007 23.410 4.070 17.355 1.0014.28 N ATOM 34 CE1 HIS A1007 22.537 3.108 17.102 1.00 15.47 C ATOM 35NE2 HIS A1007 22.214 2.526 18.245 1.00 15.49 N ATOM 36 C HIS A100723.025 7.000 18.999 1.00 13.90 C ATOM 37 O HIS A1007 22.588 7.310 20.1151.00 13.25 O ATOM 38 N GLY A1008 22.276 7.053 17.888 1.00 13.72 N ATOM39 CA GLY A1008 20.870 7.476 17.931 1.00 13.61 C ATOM 40 C GLY A100819.944 6.833 16.890 1.00 13.86 C ATOM 41 O GLY A1008 20.402 6.498 15.7951.00 13.86 O ATOM 42 N ILE A1009 18.653 6.649 17.218 1.00 13.29 N ATOM43 CA ILE A1009 17.672 6.046 16.281 1.00 13.44 C ATOM 44 CB ILE A100917.342 4.554 16.639 1.00 14.13 C ATOM 45 CG2 ILE A1009 18.619 3.69616.642 1.00 13.71 C ATOM 46 CG1 ILE A1009 16.638 4.503 18.003 1.00 13.45C ATOM 47 CD1 ILE A1009 16.175 3.134 18.434 1.00 15.16 C ATOM 48 C ILEA1009 16.318 6.799 16.257 1.00 14.09 C ATOM 49 O ILE A1009 16.033 7.58917.165 1.00 12.83 O ATOM 50 N ASP A1010 15.491 6.537 15.232 1.00 14.68 NATOM 51 CA ASP A1010 14.161 7.167 15.101 1.00 16.24 C ATOM 52 CB ASPA1010 14.287 8.580 14.496 1.00 17.11 C ATOM 53 CG ASP A1010 12.944 9.32814.428 1.00 19.40 C ATOM 54 OD1 ASP A1010 12.265 9.295 13.369 1.00 19.82O ATOM 55 OD2 ASP A1010 12.563 9.948 15.446 1.00 19.26 O ATOM 56 C ASPA1010 13.193 6.348 14.230 1.00 16.72 C ATOM 57 O ASP A1010 13.618 5.69313.276 1.00 16.89 O ATOM 58 N ILE A1011 11.900 6.387 14.570 1.00 17.01 NATOM 59 CA ILE A1011 10.850 5.706 13.796 1.00 17.33 C ATOM 60 CB ILEA1011 10.410 4.353 14.447 1.00 18.10 C ATOM 61 CG2 ILE A1011 9.963 4.57015.898 1.00 17.28 C ATOM 62 CG1 ILE A1011 9.297 3.717 13.601 1.00 18.21C ATOM 63 CD1 ILE A1011 8.852 2.338 14.083 1.00 20.73 C ATOM 64 C ILEA1011 9.648 6.664 13.679 1.00 18.00 C ATOM 65 O ILE A1011 9.262 7.29814.663 1.00 16.80 O ATOM 66 N GLU A1012 9.060 6.760 12.481 1.00 18.22 NATOM 67 CA GLU A1012 7.951 7.690 12.220 1.00 19.38 C ATOM 68 CB GLUA1012 8.537 8.972 11.609 1.00 20.91 C ATOM 69 CG GLU A1012 7.537 10.03611.186 1.00 23.69 C ATOM 70 CD GLU A1012 7.065 10.909 12.336 1.00 24.81C ATOM 71 OE1 GLU A1012 7.432 10.632 13.499 1.00 24.64 O ATOM 72 OE2 GLUA1012 6.318 11.878 12.070 1.00 27.04 O ATOM 73 C GLU A1012 6.845 7.14611.293 1.00 19.45 C ATOM 74 O GLU A1012 7.119 6.397 10.358 1.00 17.84 OATOM 75 N GLU A1013 5.599 7.538 11.557 1.00 20.13 N ATOM 76 CA GLU A10134.456 7.119 10.735 1.00 21.62 C ATOM 77 CB GLU A1013 3.178 7.146 11.5841.00 24.29 C ATOM 78 CG GLU A1013 1.916 6.753 10.845 1.00 28.34 C ATOM79 CD GLU A1013 0.710 6.656 11.766 1.00 30.69 C ATOM 80 OE1 GLU A1013−0.400 6.361 11.267 1.00 33.13 O ATOM 81 OE2 GLU A1013 0.871 6.87212.990 1.00 33.49 O ATOM 82 C GLU A1013 4.302 8.061 9.521 1.00 21.59 CATOM 83 O GLU A1013 4.247 9.280 9.682 1.00 20.05 O ATOM 84 N LEU A10144.223 7.493 8.316 1.00 21.61 N ATOM 85 CA LEU A1014 4.104 8.288 7.0871.00 22.02 C ATOM 86 CB LEU A1014 4.191 7.365 5.857 1.00 23.16 C ATOM 87CG LEU A1014 5.502 6.571 5.745 1.00 24.38 C ATOM 88 CD1 LEU A1014 5.4545.622 4.551 1.00 25.08 C ATOM 89 CD2 LEU A1014 6.667 7.538 5.604 1.0025.38 C ATOM 90 C LEU A1014 2.841 9.158 7.006 1.00 22.02 C ATOM 91 O LEUA1014 2.867 10.240 6.419 1.00 21.55 O ATOM 92 N ALA A1015 1.742 8.6917.593 1.00 22.06 N ATOM 93 CA ALA A1015 0.488 9.452 7.595 1.00 22.62 CATOM 94 CB ALA A1015 −0.605 8.656 8.299 1.00 22.21 C ATOM 95 C ALA A10150.644 10.817 8.274 1.00 22.87 C ATOM 96 O ALA A1015 0.005 11.796 7.8751.00 23.00 O ATOM 97 N SER A1016 1.482 10.876 9.307 1.00 23.27 N ATOM 98CA SER A1016 1.716 12.123 10.034 1.00 23.77 C ATOM 99 CB SER A1016 2.53511.860 11.305 1.00 24.30 C ATOM 100 OG SER A1016 1.890 10.919 12.1451.00 26.09 O ATOM 101 C SER A1016 2.443 13.146 9.162 1.00 23.41 C ATOM102 O SER A1016 2.173 14.348 9.249 1.00 23.19 O ATOM 103 N ILE A10173.378 12.673 8.340 1.00 23.05 N ATOM 104 CA ILE A1017 4.118 13.566 7.4501.00 22.92 C ATOM 105 CB ILE A1017 5.355 12.860 6.838 1.00 23.00 C ATOM106 CG2 ILE A1017 6.107 13.823 5.918 1.00 23.26 C ATOM 107 CG1 ILE A10176.289 12.365 7.951 1.00 23.63 C ATOM 108 CD1 ILE A1017 6.896 13.4678.810 1.00 22.84 C ATOM 109 C ILE A1017 3.204 14.053 6.308 1.00 23.44 CATOM 110 O ILE A1017 3.276 15.218 5.896 1.00 23.11 O ATOM 111 N GLUA1018 2.341 13.170 5.805 1.00 22.98 N ATOM 112 CA GLU A1018 1.443 13.5494.714 1.00 24.09 C ATOM 113 CB GLU A1018 0.729 12.306 4.147 1.00 25.23 CATOM 114 CG GLU A1018 −0.252 12.592 2.997 1.00 27.75 C ATOM 115 CD GLUA1018 −0.632 11.345 2.190 1.00 29.64 C ATOM 116 OE1 GLU A1018 −0.80710.255 2.783 1.00 30.50 O ATOM 117 OE2 GLU A1018 −0.771 11.459 0.9521.00 30.61 O ATOM 118 C GLU A1018 0.427 14.612 5.150 1.00 24.15 C ATOM119 O GLU A1018 0.142 15.550 4.395 1.00 23.68 O ATOM 120 N SER A1019−0.103 14.481 6.367 1.00 23.86 N ATOM 121 CA SER A1019 −1.078 15.4456.879 1.00 24.87 C ATOM 122 CB SER A1019 −1.641 14.993 8.234 1.00 24.60C ATOM 123 OG SER A1019 −2.387 13.794 8.120 1.00 26.37 O ATOM 124 C SERA1019 −0.450 16.824 7.045 1.00 25.06 C ATOM 125 O SER A1019 −1.07717.836 6.741 1.00 25.39 O ATOM 126 N ALA A1020 0.790 16.856 7.525 1.0025.98 N ATOM 127 CA ALA A1020 1.508 18.112 7.748 1.00 26.26 C ATOM 128CB ALA A1020 2.869 17.829 8.399 1.00 26.48 C ATOM 129 C ALA A1020 1.69518.909 6.460 1.00 26.83 C ATOM 130 O ALA A1020 1.589 20.138 6.463 1.0026.25 O ATOM 131 N VAL A1021 1.974 18.210 5.364 1.00 27.31 N ATOM 132 CAVAL A1021 2.166 18.855 4.064 1.00 28.77 C ATOM 133 CB VAL A1021 2.76717.868 3.029 1.00 28.35 C ATOM 134 CG1 VAL A1021 2.801 18.510 1.639 1.0028.63 C ATOM 135 CG2 VAL A1021 4.176 17.461 3.457 1.00 28.09 C ATOM 136C VAL A1021 0.845 19.396 3.512 1.00 30.16 C ATOM 137 O VAL A1021 0.77520.541 3.054 1.00 29.31 O ATOM 138 N THR A1022 −0.195 18.565 3.557 1.0031.76 N ATOM 139 CA THR A1022 −1.515 18.951 3.057 1.00 33.81 C ATOM 140CB THR A1022 −2.541 17.798 3.230 1.00 33.53 C ATOM 141 OG1 THR A1022−2.119 16.663 2.466 1.00 33.79 O ATOM 142 CG2 THR A1022 −3.926 18.2242.749 1.00 33.72 C ATOM 143 C THR A1022 −2.032 20.183 3.790 1.00 34.97 CATOM 144 O THR A1022 −2.802 20.968 3.237 1.00 36.01 O ATOM 145 N ARGA1023 −1.585 20.346 5.029 1.00 36.61 N ATOM 146 CA ARG A1023 −1.98821.462 5.876 1.00 38.01 C ATOM 147 CB ARG A1023 −1.371 21.297 7.267 1.0038.96 C ATOM 148 CG ARG A1023 −2.284 21.702 8.409 1.00 40.44 C ATOM 149CD ARG A1023 −2.443 20.556 9.393 1.00 41.63 C ATOM 150 NE ARG A1023−1.184 20.219 10.053 1.00 42.83 N ATOM 151 CZ ARG A1023 −1.000 19.13410.800 1.00 43.45 C ATOM 152 NH1 ARG A1023 −1.997 18.277 10.981 1.0043.85 N ATOM 153 NH2 ARG A1023 0.178 18.906 11.367 1.00 43.30 N ATOM 154C ARG A1023 −1.603 22.825 5.302 1.00 38.55 C ATOM 155 O ARG A1023 −2.14323.850 5.722 1.00 38.81 O ATOM 156 N HIS A1024 −0.663 22.842 4.359 1.0038.91 N ATOM 157 CA HIS A1024 −0.244 24.096 3.733 1.00 38.99 C ATOM 158CB HIS A1024 −1.432 24.654 2.935 1.00 40.09 C ATOM 159 CG HIS A1024−1.184 25.993 2.315 1.00 41.43 C ATOM 160 CD2 HIS A1024 −1.936 27.1192.304 1.00 41.88 C ATOM 161 ND1 HIS A1024 −0.058 26.276 1.573 1.00 41.78N ATOM 162 CE1 HIS A1024 −0.126 27.519 1.131 1.00 42.17 C ATOM 163 NE2HIS A1024 −1.257 28.053 1.560 1.00 42.70 N ATOM 164 C HIS A1024 0.24525.107 4.782 1.00 38.60 C ATOM 165 O HIS A1024 −0.251 26.236 4.857 1.0038.61 O ATOM 166 N GLU A1025 1.234 24.696 5.575 1.00 37.69 N ATOM 167 CAGLU A1025 1.784 25.533 6.643 1.00 36.89 C ATOM 168 CB GLU A1025 1.54524.854 7.995 1.00 37.94 C ATOM 169 CG GLU A1025 2.255 23.508 8.126 1.0039.13 C ATOM 170 CD GLU A1025 2.003 22.828 9.459 1.00 40.28 C ATOM 171OE1 GLU A1025 0.853 22.405 9.709 1.00 41.24 O ATOM 172 OE2 GLU A10252.959 22.716 10.258 1.00 40.84 O ATOM 173 C GLU A1025 3.280 25.856 6.5181.00 35.45 C ATOM 174 O GLU A1025 3.857 26.466 7.424 1.00 35.71 O ATOM175 N GLY A1026 3.906 25.441 5.420 1.00 33.22 N ATOM 176 CA GLY A10265.324 25.708 5.220 1.00 30.99 C ATOM 177 C GLY A1026 6.265 24.668 5.8191.00 29.44 C ATOM 178 O GLY A1026 7.448 24.943 6.040 1.00 28.80 O ATOM179 N PHE A1027 5.743 23.470 6.073 1.00 27.49 N ATOM 180 CA PHE A10276.524 22.378 6.657 1.00 26.42 C ATOM 181 CB PHE A1027 5.618 21.149 6.8301.00 26.50 C ATOM 182 CG PHE A1027 6.272 19.995 7.541 1.00 26.07 C ATOM183 CD1 PHE A1027 6.650 20.103 8.876 1.00 25.99 C ATOM 184 CD2 PHE A10276.499 18.790 6.873 1.00 26.17 C ATOM 185 CE1 PHE A1027 7.243 19.0289.541 1.00 26.70 C ATOM 186 CE2 PHE A1027 7.091 17.711 7.527 1.00 26.08C ATOM 187 CZ PHE A1027 7.465 17.828 8.863 1.00 26.23 C ATOM 188 C PHEA1027 7.776 21.998 5.852 1.00 25.70 C ATOM 189 O PHE A1027 8.892 22.0176.377 1.00 25.54 O ATOM 190 N ALA A1028 7.598 21.656 4.579 1.00 24.86 NATOM 191 CA ALA A1028 8.726 21.260 3.737 1.00 24.85 C ATOM 192 CB ALAA1028 8.232 20.919 2.333 1.00 24.87 C ATOM 193 C ALA A1028 9.824 22.3253.661 1.00 25.07 C ATOM 194 O ALA A1028 11.018 22.009 3.685 1.00 24.02 OATOM 195 N LYS A1029 9.417 23.587 3.571 1.00 25.80 N ATOM 196 CA LYSA1029 10.364 24.695 3.488 1.00 26.80 C ATOM 197 CB LYS A1029 9.59826.000 3.222 1.00 28.18 C ATOM 198 CG LYS A1029 10.449 27.200 2.800 1.0030.30 C ATOM 199 CD LYS A1029 11.251 27.769 3.958 1.00 32.28 C ATOM 200CE LYS A1029 11.799 29.151 3.636 1.00 33.23 C ATOM 201 NZ LYS A102910.702 30.153 3.506 1.00 34.55 N ATOM 202 C LYS A1029 11.197 24.8064.771 1.00 26.54 C ATOM 203 O LYS A1029 12.344 25.244 4.738 1.00 26.39 OATOM 204 N ARG A1030 10.624 24.394 5.897 1.00 26.43 N ATOM 205 CA ARGA1030 11.327 24.464 7.178 1.00 26.50 C ATOM 206 CB ARG A1030 10.31224.485 8.334 1.00 27.57 C ATOM 207 CG ARG A1030 10.945 24.487 9.727 1.0030.51 C ATOM 208 CD ARG A1030 9.933 24.858 10.820 1.00 31.96 C ATOM 209NE ARG A1030 8.887 23.851 11.008 1.00 32.84 N ATOM 210 CZ ARG A10309.033 22.740 11.723 1.00 33.04 C ATOM 211 NH1 ARG A1030 10.184 22.48212.327 1.00 33.30 N ATOM 212 NH2 ARG A1030 8.028 21.884 11.836 1.0033.60 N ATOM 213 C ARG A1030 12.325 23.327 7.407 1.00 25.55 C ATOM 214 OARG A1030 13.402 23.539 7.976 1.00 25.72 O ATOM 215 N VAL A1031 11.96722.130 6.952 1.00 24.16 N ATOM 216 CA VAL A1031 12.795 20.934 7.134 1.0023.09 C ATOM 217 CB VAL A1031 11.903 19.655 7.150 1.00 23.53 C ATOM 218CG1 VAL A1031 12.765 18.398 7.339 1.00 23.93 C ATOM 219 CG2 VAL A103110.874 19.754 8.258 1.00 22.96 C ATOM 220 C VAL A1031 13.932 20.6846.134 1.00 22.57 C ATOM 221 O VAL A1031 14.952 20.094 6.504 1.00 22.31 OATOM 222 N LEU A1032 13.765 21.127 4.887 1.00 21.47 N ATOM 223 CA LEUA1032 14.764 20.888 3.830 1.00 21.78 C ATOM 224 CB LEU A1032 14.06220.277 2.607 1.00 21.38 C ATOM 225 CG LEU A1032 13.126 19.073 2.773 1.0020.75 C ATOM 226 CD1 LEU A1032 12.446 18.779 1.428 1.00 21.22 C ATOM 227CD2 LEU A1032 13.912 17.851 3.249 1.00 20.06 C ATOM 228 C LEU A103215.565 22.107 3.355 1.00 22.39 C ATOM 229 O LEU A1032 15.061 23.2333.375 1.00 22.40 O ATOM 230 N THR A1033 16.806 21.875 2.917 1.00 23.26 NATOM 231 CA THR A1033 17.661 22.951 2.394 1.00 24.31 C ATOM 232 CB THRA1033 19.171 22.577 2.366 1.00 24.32 C ATOM 233 OG1 THR A1033 19.38021.472 1.473 1.00 24.43 O ATOM 234 CG2 THR A1033 19.671 22.217 3.7561.00 23.93 C ATOM 235 C THR A1033 17.255 23.215 0.945 1.00 25.20 C ATOM236 O THR A1033 16.343 22.570 0.426 1.00 24.87 O ATOM 237 N ALA A103417.937 24.158 0.297 1.00 25.70 N ATOM 238 CA ALA A1034 17.650 24.476−1.100 1.00 26.57 C ATOM 239 CB ALA A1034 18.485 25.676 −1.548 1.0027.15 C ATOM 240 C ALA A1034 17.943 23.270 −1.997 1.00 26.78 C ATOM 241O ALA A1034 17.115 22.896 −2.829 1.00 27.20 O ATOM 242 N LEU A103519.122 22.672 −1.831 1.00 26.52 N ATOM 243 CA LEU A1035 19.513 21.503−2.623 1.00 27.27 C ATOM 244 CB LEU A1035 20.943 21.063 −2.276 1.0027.34 C ATOM 245 CG LEU A1035 22.137 21.950 −2.658 1.00 28.71 C ATOM 246CD1 LEU A1035 23.388 21.443 −1.953 1.00 28.34 C ATOM 247 CD2 LEU A103522.348 21.949 −4.171 1.00 29.34 C ATOM 248 C LEU A1035 18.549 20.327−2.408 1.00 26.73 C ATOM 249 O LEU A1035 18.124 19.679 −3.369 1.00 26.11O ATOM 250 N GLU A1036 18.209 20.048 −1.151 1.00 26.36 N ATOM 251 CA GLUA1036 17.285 18.958 −0.852 1.00 26.00 C ATOM 252 CB GLU A1036 17.11918.801 0.675 1.00 24.96 C ATOM 253 CG GLU A1036 18.307 18.111 1.367 1.0022.07 C ATOM 254 CD GLU A1036 18.254 18.150 2.900 1.00 22.03 C ATOM 255OE1 GLU A1036 18.819 17.229 3.540 1.00 20.25 O ATOM 256 OE2 GLU A103617.671 19.102 3.472 1.00 19.80 O ATOM 257 C GLU A1036 15.934 19.228−1.526 1.00 27.44 C ATOM 258 O GLU A1036 15.296 18.314 −2.060 1.00 26.45O ATOM 259 N MET A1037 15.514 20.493 −1.525 1.00 28.51 N ATOM 260 CA META1037 14.242 20.888 −2.132 1.00 30.20 C ATOM 261 CB MET A1037 13.97922.377 −1.877 1.00 31.18 C ATOM 262 CG MET A1037 12.608 22.872 −2.3241.00 32.64 C ATOM 263 SD MET A1037 11.236 22.231 −1.342 1.00 35.22 SATOM 264 CE MET A1037 9.873 22.344 −2.511 1.00 34.31 C ATOM 265 C META1037 14.192 20.608 −3.637 1.00 30.82 C ATOM 266 O MET A1037 13.14120.248 −4.176 1.00 31.12 O ATOM 267 N GLU A1038 15.320 20.780 −4.3171.00 31.36 N ATOM 268 CA GLU A1038 15.371 20.526 −5.756 1.00 31.95 CATOM 269 CB GLU A1038 16.773 20.820 −6.296 1.00 33.04 C ATOM 270 CG GLUA1038 17.111 22.300 −6.367 1.00 35.12 C ATOM 271 CD GLU A1038 18.57822.550 −6.673 1.00 36.56 C ATOM 272 OE1 GLU A1038 18.943 23.713 −6.9411.00 37.89 O ATOM 273 OE2 GLU A1038 19.371 21.585 −6.639 1.00 37.49 OATOM 274 C GLU A1038 14.988 19.080 −6.072 1.00 31.21 C ATOM 275 O GLUA1038 14.268 18.816 −7.036 1.00 30.88 O ATOM 276 N ARG A1039 15.47418.151 −5.253 1.00 29.97 N ATOM 277 CA ARG A1039 15.188 16.730 −5.4271.00 28.84 C ATOM 278 CB ARG A1039 16.086 15.913 −4.483 1.00 29.69 CATOM 279 CG ARG A1039 15.853 14.402 −4.480 1.00 31.09 C ATOM 280 CD ARGA1039 16.329 13.727 −5.758 1.00 32.23 C ATOM 281 NE ARG A1039 16.12512.280 −5.708 1.00 33.37 N ATOM 282 CZ ARG A1039 16.076 11.492 −6.7801.00 33.30 C ATOM 283 NH1 ARG A1039 16.222 12.007 −7.992 1.00 33.19 NATOM 284 NH2 ARG A1039 15.852 10.191 −6.641 1.00 32.92 N ATOM 285 C ARGA1039 13.709 16.442 −5.145 1.00 27.71 C ATOM 286 O ARG A1039 13.05915.705 −5.887 1.00 26.61 O ATOM 287 N PHE A1040 13.189 17.041 −4.0761.00 26.75 N ATOM 288 CA PHE A1040 11.795 16.867 −3.659 1.00 26.16 CATOM 289 CB PHE A1040 11.532 17.729 −2.405 1.00 25.81 C ATOM 290 CG PHEA1040 10.111 17.665 −1.886 1.00 25.91 C ATOM 291 CD1 PHE A1040 9.61516.508 −1.292 1.00 25.16 C ATOM 292 CD2 PHE A1040 9.275 18.778 −1.9791.00 25.61 C ATOM 293 CE1 PHE A1040 8.309 16.457 −0.798 1.00 25.37 CATOM 294 CE2 PHE A1040 7.966 18.740 −1.490 1.00 25.17 C ATOM 295 CZ PHEA1040 7.481 17.579 −0.897 1.00 25.69 C ATOM 296 C PHE A1040 10.78217.210 −4.760 1.00 25.80 C ATOM 297 O PHE A1040 9.835 16.460 −4.990 1.0025.42 O ATOM 298 N THR A1041 10.984 18.332 −5.443 1.00 25.73 N ATOM 299CA THR A1041 10.053 18.759 −6.493 1.00 26.24 C ATOM 300 CB THR A104110.257 20.259 −6.836 1.00 26.86 C ATOM 301 OG1 THR A1041 11.634 20.507−7.154 1.00 26.58 O ATOM 302 CG2 THR A1041 9.849 21.130 −5.656 1.0026.06 C ATOM 303 C THR A1041 10.066 17.948 −7.800 1.00 26.59 C ATOM 304O THR A1041 9.149 18.071 −8.620 1.00 27.01 O ATOM 305 N SER A1042 11.08017.111 −7.996 1.00 26.31 N ATOM 306 CA SER A1042 11.158 16.305 −9.2221.00 26.03 C ATOM 307 CB SER A1042 12.618 16.106 −9.631 1.00 26.30 CATOM 308 OG SER A1042 13.287 15.231 −8.737 1.00 27.19 O ATOM 309 C SERA1042 10.488 14.935 −9.082 1.00 25.97 C ATOM 310 O SER A1042 10.35414.198 −10.063 1.00 25.27 O ATOM 311 N LEU A1043 10.064 14.599 −7.8651.00 25.25 N ATOM 312 CA LEU A1043 9.431 13.310 −7.601 1.00 25.51 C ATOM313 CB LEU A1043 9.906 12.765 −6.245 1.00 24.11 C ATOM 314 CG LEU A104311.425 12.571 −6.118 1.00 24.06 C ATOM 315 CD1 LEU A1043 11.768 12.080−4.715 1.00 22.60 C ATOM 316 CD2 LEU A1043 11.914 11.571 −7.164 1.0023.86 C ATOM 317 C LEU A1043 7.907 13.389 −7.634 1.00 25.82 C ATOM 318 OLEU A1043 7.333 14.475 −7.575 1.00 26.42 O ATOM 319 N LYS A1044 7.25612.233 −7.723 1.00 26.67 N ATOM 320 CA LYS A1044 5.802 12.184 −7.7851.00 27.60 C ATOM 321 CB LYS A1044 5.361 11.803 −9.200 1.00 29.18 C ATOM322 CG LYS A1044 5.705 10.369 −9.562 1.00 31.06 C ATOM 323 CD LYS A10445.359 10.045 −10.999 1.00 32.81 C ATOM 324 CE LYS A1044 5.572 8.567−11.282 1.00 33.54 C ATOM 325 NZ LYS A1044 4.702 7.716 −10.419 1.0034.84 N ATOM 326 C LYS A1044 5.159 11.211 −6.795 1.00 27.94 C ATOM 327 OLYS A1044 5.774 10.227 −6.367 1.00 27.61 O ATOM 328 N GLY A1045 3.90411.500 −6.464 1.00 27.68 N ATOM 329 CA GLY A1045 3.124 10.671 −5.5621.00 28.74 C ATOM 330 C GLY A1045 3.741 10.224 −4.252 1.00 28.99 C ATOM331 O GLY A1045 4.282 11.024 −3.487 1.00 29.00 O ATOM 332 N ARG A10463.643 8.925 −3.998 1.00 29.30 N ATOM 333 CA ARG A1046 4.155 8.320 −2.7761.00 30.48 C ATOM 334 CB ARG A1046 3.790 6.833 −2.754 1.00 32.57 C ATOM335 CG ARG A1046 3.044 6.390 −1.513 1.00 35.84 C ATOM 336 CD ARG A10462.680 4.922 −1.598 1.00 38.51 C ATOM 337 NE ARG A1046 2.023 4.445 −0.3841.00 41.12 N ATOM 338 CZ ARG A1046 1.613 3.194 −0.204 1.00 42.33 C ATOM339 NH1 ARG A1046 1.024 2.842 0.931 1.00 42.60 N ATOM 340 NH2 ARG A10461.793 2.292 −1.164 1.00 43.25 N ATOM 341 C ARG A1046 5.663 8.479 −2.5821.00 29.60 C ATOM 342 O ARG A1046 6.128 8.686 −1.460 1.00 28.95 O ATOM343 N ARG A1047 6.423 8.375 −3.668 1.00 28.70 N ATOM 344 CA ARG A10477.875 8.495 −3.585 1.00 28.01 C ATOM 345 CD ARG A1047 8.512 8.167 −4.9431.00 29.65 C ATOM 346 CG ARG A1047 9.566 7.069 −4.869 1.00 32.09 C ATOM347 CD ARG A1047 9.831 6.426 −6.228 1.00 34.53 C ATOM 348 NE ARG A10478.601 5.910 −6.825 1.00 36.57 N ATOM 349 CZ ARG A1047 8.548 5.138 −7.9061.00 37.35 C ATOM 350 NH1 ARG A1047 7.373 4.727 −8.368 1.00 38.05 N ATOM351 NH2 ARG A1047 9.663 4.767 −8.523 1.00 38.02 N ATOM 352 C ARG A10478.288 9.890 −3.117 1.00 26.86 C ATOM 353 O ARG A1047 9.309 10.048 −2.4441.00 25.61 O ATOM 354 N GLN A1048 7.481 10.891 −3.464 1.00 25.04 N ATOM355 CA GLN A1048 7.739 12.277 −3.079 1.00 24.33 C ATOM 356 CB GLN A10486.733 13.217 −3.779 1.00 25.19 C ATOM 357 CG GLN A1048 7.138 14.694−3.774 1.00 26.24 C ATOM 358 CD GLN A1048 6.221 15.581 −4.620 1.00 26.41C ATOM 359 OE1 GLN A1048 6.617 16.664 −5.047 1.00 26.86 O ATOM 360 NE2GLN A1048 4.994 15.127 −4.853 1.00 27.01 N ATOM 361 C GLN A1048 7.63212.442 −1.553 1.00 23.25 C ATOM 362 O GLN A1048 8.463 13.110 −0.935 1.0023.01 O ATOM 363 N ILE A1049 6.615 11.830 −0.949 1.00 22.49 N ATOM 364CA ILE A1049 6.423 11.919 0.504 1.00 22.00 C ATOM 365 CB ILE A1049 5.01111.414 0.916 1.00 23.38 C ATOM 366 CG2 ILE A1049 4.810 11.564 2.421 1.0023.48 C ATOM 367 CG1 ILE A1049 3.928 12.197 0.161 1.00 24.39 C ATOM 368CD1 ILE A1049 3.923 13.695 0.424 1.00 25.65 C ATOM 369 C ILE A1049 7.49611.118 1.274 1.00 21.25 C ATOM 370 O ILE A1049 7.940 11.537 2.347 1.0019.66 O ATOM 371 N GLU A1050 7.913 9.975 0.724 1.00 20.69 N ATOM 372 CAGLU A1050 8.939 9.146 1.372 1.00 20.67 C ATOM 373 CB GLU A1050 9.0937.794 0.650 1.00 22.03 C ATOM 374 CG GLU A1050 10.362 7.017 1.051 1.0023.69 C ATOM 375 CD GLU A1050 10.385 6.625 2.520 1.00 24.98 C ATOM 376OE1 GLU A1050 11.498 6.519 3.095 1.00 23.91 O ATOM 377 OE2 GLU A10509.292 6.409 3.097 1.00 25.89 O ATOM 378 C GLU A1050 10.298 9.851 1.4301.00 19.72 C ATOM 379 O GLU A1050 11.073 9.634 2.367 1.00 19.12 O ATOM380 N TYR A1051 10.604 10.680 0.431 1.00 18.43 N ATOM 381 CA TYR A105111.878 11.400 0.435 1.00 17.86 C ATOM 382 CB TYR A1051 12.110 12.129−0.902 1.00 18.12 C ATOM 383 CG TYR A1051 13.379 12.970 −0.932 1.0017.88 C ATOM 384 CD1 TYR A1051 13.372 14.307 −0.518 1.00 17.74 C ATOM385 CE1 TYR A1051 14.547 15.076 −0.516 1.00 17.82 C ATOM 386 CD2 TYRA1051 14.592 12.419 −1.345 1.00 17.56 C ATOM 387 CE2 TYR A1051 15.77013.176 −1.344 1.00 18.21 C ATOM 388 CZ TYR A1051 15.740 14.501 −0.9291.00 18.16 C ATOM 389 OH TYR A1051 16.908 15.237 −0.923 1.00 18.28 OATOM 390 C TYR A1051 11.915 12.409 1.590 1.00 17.91 C ATOM 391 O TYRA1051 12.927 12.525 2.290 1.00 16.53 O ATOM 392 N LEU A1052 10.81013.137 1.778 1.00 17.38 N ATOM 393 CA LEU A1052 10.709 14.131 2.851 1.0017.07 C ATOM 394 CB LEU A1052 9.392 14.917 2.731 1.00 17.53 C ATOM 395CG LEU A1052 8.985 15.844 3.890 1.00 17.80 C ATOM 396 CD1 LEU A105210.096 16.844 4.191 1.00 18.32 C ATOM 397 CD2 LEU A1052 7.693 16.5733.524 1.00 17.67 C ATOM 398 C LEU A1052 10.784 13.448 4.219 1.00 16.62 CATOM 399 O LEU A1052 11.544 13.874 5.093 1.00 16.61 O ATOM 400 N ALAA1053 10.006 12.383 4.394 1.00 15.83 N ATOM 401 CA ALA A1053 9.98511.645 5.662 1.00 15.97 C ATOM 402 CB ALA A1053 8.974 10.516 5.587 1.0015.80 C ATOM 403 C ALA A1053 11.362 11.091 6.038 1.00 15.64 C ATOM 404 OALA A1053 11.750 11.129 7.208 1.00 15.53 O ATOM 405 N GLY A1054 12.09410.573 5.054 1.00 14.85 N ATOM 406 CA GLY A1054 13.420 10.028 5.327 1.0014.89 C ATOM 407 C GLY A1054 14.431 11.073 5.789 1.00 14.97 C ATOM 408 OGLY A1054 15.243 10.820 6.689 1.00 14.15 O ATOM 409 N ARG A1055 14.40312.250 5.169 1.00 14.68 N ATOM 410 CA ARG A1055 15.327 13.313 5.553 1.0015.29 C ATOM 411 CB ARG A1055 15.257 14.462 4.533 1.00 14.70 C ATOM 412CG ARG A1055 16.364 14.420 3.438 1.00 16.14 C ATOM 413 CD ARG A105516.452 13.082 2.658 1.00 16.61 C ATOM 414 NE ARG A1055 17.610 13.0391.745 1.00 16.90 N ATOM 415 CZ ARG A1055 17.966 11.976 1.021 1.00 17.56C ATOM 416 NH1 ARG A1055 17.265 10.850 1.093 1.00 16.02 N ATOM 417 NH2ARG A1055 19.028 12.034 0.215 1.00 18.06 N ATOM 418 C ARG A1055 15.01013.804 6.980 1.00 15.61 C ATOM 419 O ARG A1055 15.909 14.138 7.755 1.0015.05 O ATOM 420 N TRP A1056 13.731 13.826 7.333 1.00 15.92 N ATOM 421CA TRP A1056 13.324 14.252 8.676 1.00 17.44 C ATOM 422 CB TRP A105611.791 14.409 8.706 1.00 20.42 C ATOM 423 CG TRP A1056 11.151 14.20210.044 1.00 24.52 C ATOM 424 CD2 TRP A1056 10.650 15.212 10.921 1.0026.47 C ATOM 425 CE2 TRP A1056 10.140 14.556 12.065 1.00 27.71 C ATOM426 CE3 TRP A1056 10.581 16.607 10.854 1.00 27.13 C ATOM 427 CD1 TRPA1056 10.931 13.005 10.673 1.00 25.93 C ATOM 428 NE1 TRP A1056 10.32513.211 11.885 1.00 27.77 N ATOM 429 CZ2 TRP A1056 9.567 15.250 13.1331.00 28.62 C ATOM 430 CZ3 TRP A1056 10.012 17.297 11.915 1.00 28.11 CATOM 431 CH2 TRP A1056 9.512 16.617 13.041 1.00 29.24 C ATOM 432 C TRPA1056 13.807 13.259 9.758 1.00 16.63 C ATOM 433 O TRP A1056 14.33913.661 10.813 1.00 14.62 O ATOM 434 N SER A1057 13.645 11.965 9.477 1.0015.34 N ATOM 435 CA SER A1057 14.034 10.892 10.404 1.00 14.89 C ATOM 436CB SER A1057 13.509 9.549 9.864 1.00 16.31 C ATOM 437 OG SER A105713.653 8.482 10.792 1.00 15.29 O ATOM 438 C SER A1057 15.558 10.83310.624 1.00 14.80 C ATOM 439 O SER A1057 16.033 10.618 11.748 1.00 13.11O ATOM 440 N ALA A1058 16.326 11.043 9.560 1.00 13.86 N ATOM 441 CA ALAA1058 17.784 11.015 9.670 1.00 14.03 C ATOM 442 CB ALA A1058 18.40811.077 8.283 1.00 14.39 C ATOM 443 C ALA A1058 18.326 12.162 10.528 1.0014.15 C ATOM 444 O ALA A1058 19.253 11.972 11.326 1.00 12.67 O ATOM 445N LYS A1059 17.760 13.356 10.346 1.00 14.25 N ATOM 446 CA LYS A105918.198 14.530 11.102 1.00 14.94 C ATOM 447 CB LYS A1059 17.561 15.80710.511 1.00 14.63 C ATOM 448 CG LYS A1059 18.030 16.077 9.061 1.00 15.21C ATOM 449 CD LYS A1059 17.605 17.445 8.497 1.00 14.78 C ATOM 450 CE LYSA1059 18.198 17.662 7.096 1.00 15.27 C ATOM 451 NZ LYS A1059 17.78018.955 6.460 1.00 14.73 N ATOM 452 C LYS A1059 17.902 14.382 12.597 1.0015.88 C ATOM 453 O LYS A1059 18.726 14.755 13.441 1.00 15.17 O ATOM 454N GLU A1060 16.743 13.819 12.933 1.00 15.81 N ATOM 455 CA GLU A106016.395 13.609 14.337 1.00 16.66 C ATOM 456 CB GLU A1060 14.943 13.14214.474 1.00 18.92 C ATOM 457 CG GLU A1060 13.922 14.183 14.023 1.0023.44 C ATOM 458 CD GLU A1060 12.804 14.369 15.031 1.00 26.75 C ATOM 459OE1 GLU A1060 12.175 13.358 15.414 1.00 29.16 O ATOM 460 OE2 GLU A106012.547 15.522 15.437 1.00 27.98 O ATOM 461 C GLU A1060 17.333 12.57814.977 1.00 15.69 C ATOM 462 O GLU A1060 17.740 12.730 16.138 1.00 14.40O ATOM 463 N ALA A1061 17.689 11.541 14.219 1.00 14.51 N ATOM 464 CA ALAA1061 18.586 10.500 14.727 1.00 14.88 C ATOM 465 CB ALA A1061 18.6589.312 13.730 1.00 14.28 C ATOM 466 C ALA A1061 19.998 11.037 15.018 1.0015.17 C ATOM 467 O ALA A1061 20.635 10.622 16.001 1.00 14.05 O ATOM 468N PHE A1062 20.488 11.943 14.167 1.00 14.78 N ATOM 469 CA PHE A106221.811 12.545 14.365 1.00 16.06 C ATOM 470 CB PHE A1062 22.200 13.43313.161 1.00 16.25 C ATOM 471 CG PHE A1062 23.514 14.176 13.341 1.0017.02 C ATOM 472 CD1 PHE A1062 23.562 15.384 14.039 1.00 17.84 C ATOM473 CD2 PHE A1062 24.707 13.642 12.847 1.00 16.96 C ATOM 474 CE1 PHEA1062 24.783 16.049 14.247 1.00 17.77 C ATOM 475 CE2 PHE A1062 25.93114.297 13.049 1.00 17.84 C ATOM 476 CZ PHE A1062 25.964 15.505 13.7541.00 18.67 C ATOM 477 C PHE A1062 21.830 13.380 15.651 1.00 16.47 C ATOM478 O PHE A1062 22.792 13.326 16.422 1.00 15.43 O ATOM 479 N SER A106320.760 14.138 15.895 1.00 17.69 N ATOM 480 CA SER A1063 20.695 14.97917.093 1.00 19.00 C ATOM 481 CB SER A1063 19.446 15.881 17.067 1.0020.22 C ATOM 482 OG SER A1063 18.276 15.162 17.434 1.00 23.89 O ATOM 483C SER A1063 20.707 14.148 18.383 1.00 19.17 C ATOM 484 O SER A106321.229 14.602 19.405 1.00 19.65 O ATOM 485 N LYS A1064 20.124 12.94918.353 1.00 18.93 N ATOM 486 CA LYS A1064 20.121 12.093 19.545 1.0019.27 C ATOM 487 CB LYS A1064 19.094 10.961 19.418 1.00 19.83 C ATOM 488CG LYS A1064 17.648 11.413 19.471 1.00 21.72 C ATOM 489 CD LYS A106416.720 10.201 19.456 1.00 23.02 C ATOM 490 CE LYS A1064 15.270 10.61419.240 1.00 24.30 C ATOM 491 NZ LYS A1064 14.379 9.425 19.074 1.00 25.01N ATOM 492 C LYS A1064 21.510 11.497 19.770 1.00 19.33 C ATOM 493 O LYSA1064 21.920 11.256 20.922 1.00 18.44 O ATOM 494 N ALA A1065 22.23011.254 18.674 1.00 18.91 N ATOM 495 CA ALA A1065 23.588 10.716 18.7571.00 20.48 C ATOM 496 CB ALA A1065 24.110 10.348 17.359 1.00 19.55 CATOM 497 C ALA A1065 24.515 11.745 19.417 1.00 22.05 C ATOM 498 O ALAA1065 25.486 11.374 20.086 1.00 22.04 O ATOM 499 N MET A1066 24.22413.032 19.224 1.00 23.48 N ATOM 500 CA MET A1066 25.027 14.101 19.8361.00 26.32 C ATOM 501 CB MET A1066 24.893 15.409 19.044 1.00 27.55 CATOM 502 CG MET A1066 25.471 15.377 17.634 1.00 29.85 C ATOM 503 SD META1066 27.227 15.839 17.541 1.00 34.49 S ATOM 504 CE MET A1066 27.10017.585 17.194 1.00 32.80 C ATOM 505 C MET A1066 24.554 14.334 21.2771.00 27.22 C ATOM 506 O MET A1066 25.272 14.916 22.093 1.00 27.02 O ATOM507 N GLY A1067 23.335 13.885 21.572 1.00 28.21 N ATOM 508 CA GLY A106722.770 14.032 22.905 1.00 29.77 C ATOM 509 C GLY A1067 22.161 15.39523.194 1.00 31.30 C ATOM 510 O GLY A1067 21.943 15.746 24.356 1.00 30.88O ATOM 511 N THR A1068 21.857 16.153 22.145 1.00 32.65 N ATOM 512 CA THRA1068 21.305 17.495 22.309 1.00 34.08 C ATOM 513 CB THR A1068 22.12818.520 21.510 1.00 34.54 C ATOM 514 OG1 THR A1068 21.950 18.280 20.1091.00 34.50 O ATOM 515 CG2 THR A1068 23.613 18.400 21.849 1.00 34.68 CATOM 516 C THR A1068 19.843 17.694 21.911 1.00 35.08 C ATOM 517 O THRA1068 19.199 18.637 22.380 1.00 35.34 O ATOM 518 N GLY A1069 19.32016.834 21.046 1.00 35.84 N ATOM 519 CA GLY A1069 17.942 16.995 20.6111.00 37.37 C ATOM 520 C GLY A1069 17.855 18.092 19.561 1.00 38.51 C ATOM521 O GLY A1069 18.739 18.946 19.478 1.00 38.69 O ATOM 522 N ILE A107016.801 18.088 18.752 1.00 39.34 N ATOM 523 CA ILE A1070 16.688 19.10817.722 1.00 40.39 C ATOM 524 CB ILE A1070 16.453 18.482 16.329 1.0040.56 C ATOM 525 CG2 ILE A1070 15.019 17.992 16.207 1.00 40.43 C ATOM526 CG1 ILE A1070 16.784 19.515 15.245 1.00 40.90 C ATOM 527 CD1 ILEA1070 16.900 18.947 13.841 1.00 40.92 C ATOM 528 C ILE A1070 15.61620.147 18.019 1.00 41.07 C ATOM 529 O ILE A1070 14.461 19.826 18.3051.00 41.30 O ATOM 530 N SER A1071 16.046 21.398 17.936 1.00 41.96 N ATOM531 CA SER A1071 15.247 22.588 18.201 1.00 42.87 C ATOM 532 CB SER A107114.184 22.325 19.271 1.00 43.28 C ATOM 533 OG SER A1071 14.779 21.93720.496 1.00 44.51 O ATOM 534 C SER A1071 16.314 23.521 18.753 1.00 43.09C ATOM 535 O SER A1071 16.254 24.741 18.585 1.00 43.47 O ATOM 536 N LYSA1072 17.295 22.914 19.419 1.00 42.86 N ATOM 537 CA LYS A1072 18.42723.637 19.982 1.00 42.57 C ATOM 538 CB LYS A1072 19.143 22.768 21.0221.00 42.32 C ATOM 539 CG LYS A1072 18.214 22.218 22.093 0.05 42.40 CATOM 540 CD LYS A1072 17.501 23.339 22.829 0.05 42.37 C ATOM 541 CE LYSA1072 16.446 22.789 23.773 0.05 42.36 C ATOM 542 NZ LYS A1072 15.70823.878 24.472 0.05 42.34 N ATOM 543 C LYS A1072 19.330 23.904 18.7831.00 42.27 C ATOM 544 O LYS A1072 20.222 24.752 18.814 1.00 42.17 O ATOM545 N LEU A1073 19.065 23.149 17.723 1.00 41.69 N ATOM 546 CA LEU A107319.773 23.255 16.458 1.00 41.03 C ATOM 547 CB LEU A1073 20.879 22.19716.365 1.00 41.27 C ATOM 548 CG LEU A1073 21.578 22.058 15.008 1.0041.68 C ATOM 549 CD1 LEU A1073 23.024 21.623 15.193 1.00 41.49 C ATOM550 CD2 LEU A1073 20.819 21.060 14.156 1.00 41.59 C ATOM 551 C LEU A107318.696 23.006 15.408 1.00 39.74 C ATOM 552 O LEU A1073 17.999 21.99415.458 1.00 40.51 O ATOM 553 N GLY A1074 18.550 23.937 14.473 1.00 37.90N ATOM 554 CA GLY A1074 17.532 23.795 13.452 1.00 34.96 C ATOM 555 C GLYA1074 17.853 22.756 12.399 1.00 32.76 C ATOM 556 O GLY A1074 18.96822.237 12.331 1.00 31.86 O ATOM 557 N PHE A1075 16.861 22.447 11.5751.00 30.76 N ATOM 558 CA PHE A1075 17.047 21.474 10.510 1.00 29.13 CATOM 559 CB PHE A1075 15.691 21.061 9.913 1.00 28.59 C ATOM 560 CG PHEA1075 14.795 20.317 10.871 1.00 28.14 C ATOM 561 CD1 PHE A1075 14.12920.990 11.893 1.00 28.80 C ATOM 562 CD2 PHE A1075 14.617 18.940 10.7471.00 27.48 C ATOM 563 CE1 PHE A1075 13.294 20.301 12.780 1.00 28.53 CATOM 564 CE2 PHE A1075 13.787 18.239 11.624 1.00 28.38 C ATOM 565 CZ PHEA1075 13.123 18.921 12.644 1.00 28.31 C ATOM 566 C PHE A1075 17.94022.039 9.402 1.00 27.80 C ATOM 567 O PHE A1075 18.556 21.280 8.655 1.0027.44 O ATOM 568 N GLN A1076 18.022 23.366 9.301 1.00 26.94 N ATOM 569CA GLN A1076 18.828 24.003 8.250 1.00 26.57 C ATOM 570 CB GLN A107618.468 25.490 8.111 1.00 27.23 C ATOM 571 CG GLN A1076 17.037 25.7837.655 1.00 28.06 C ATOM 572 CD GLN A1076 16.725 25.253 6.261 1.00 28.68C ATOM 573 OE1 GLN A1076 17.504 25.432 5.321 1.00 28.59 O ATOM 574 NE2GLN A1076 15.571 24.616 6.119 1.00 28.78 N ATOM 575 C GLN A1076 20.34123.880 8.435 1.00 26.18 C ATOM 576 O GLN A1076 21.110 24.292 7.565 1.0025.59 O ATOM 577 N ASP A1077 20.774 23.318 9.558 1.00 25.77 N ATOM 578CA ASP A1077 22.204 23.158 9.808 1.00 25.68 C ATOM 579 CB ASP A107722.498 23.399 11.287 1.00 28.73 C ATOM 580 CG ASP A1077 23.952 23.69711.542 1.00 30.84 C ATOM 581 OD1 ASP A1077 24.457 24.688 10.969 1.0033.09 O ATOM 582 OD2 ASP A1077 24.590 22.947 12.309 1.00 32.53 O ATOM583 C ASP A1077 22.729 21.770 9.393 1.00 24.42 C ATOM 584 O ASP A107723.928 21.487 9.516 1.00 23.80 O ATOM 585 N LEU A1078 21.831 20.9198.899 1.00 22.23 N ATOM 586 CA LEU A1078 22.187 19.559 8.463 1.00 20.68C ATOM 587 CB LEU A1078 21.530 18.525 9.398 1.00 19.99 C ATOM 588 CG LEUA1078 21.781 18.646 10.911 1.00 19.68 C ATOM 589 CD1 LEU A1078 20.85317.703 11.686 1.00 19.87 C ATOM 590 CD2 LEU A1078 23.241 18.328 11.2211.00 20.17 C ATOM 591 C LEU A1078 21.706 19.326 7.022 1.00 20.16 C ATOM592 O LEU A1078 20.708 19.915 6.605 1.00 19.88 O ATOM 593 N GLU A107922.408 18.474 6.265 1.00 19.89 N ATOM 594 CA GLU A1079 22.021 18.1654.875 1.00 18.83 C ATOM 595 CB GLU A1079 22.690 19.153 3.905 1.00 19.73C ATOM 596 CG GLU A1079 22.172 19.085 2.459 1.00 21.03 C ATOM 597 CD GLUA1079 22.914 20.028 1.510 1.00 22.47 C ATOM 598 OE1 GLU A1079 24.12719.815 1.271 1.00 22.27 O ATOM 599 OE2 GLU A1079 22.279 20.982 1.0021.00 23.12 O ATOM 600 C GLU A1079 22.385 16.716 4.484 1.00 18.06 C ATOM601 O GLU A1079 23.492 16.242 4.778 1.00 17.37 O ATOM 602 N VAL A108021.451 16.023 3.826 1.00 16.74 N ATOM 603 CA VAL A1080 21.644 14.6263.396 1.00 16.37 C ATOM 604 CB VAL A1080 20.633 13.675 4.138 1.00 16.24C ATOM 605 CG1 VAL A1080 20.859 12.217 3.738 1.00 16.31 C ATOM 606 CG2VAL A1080 20.776 13.832 5.654 1.00 16.73 C ATOM 607 C VAL A1080 21.45414.439 1.868 1.00 16.11 C ATOM 608 O VAL A1080 20.356 14.635 1.357 1.0016.59 O ATOM 609 N LEU A1081 22.519 14.060 1.155 1.00 16.23 N ATOM 610CA LEU A1081 22.473 13.830 −0.303 1.00 16.11 C ATOM 611 CB LEU A108123.488 14.749 −1.017 1.00 16.03 C ATOM 612 CG LEU A1081 23.400 16.265−0.767 1.00 17.13 C ATOM 613 CD1 LEU A1081 24.565 16.983 −1.464 1.0016.85 C ATOM 614 CD2 LEU A1081 22.064 16.798 −1.283 1.00 17.61 C ATOM615 C LEU A1081 22.790 12.350 −0.624 1.00 16.47 C ATOM 616 O LEU A108122.881 11.530 0.285 1.00 15.85 O ATOM 617 N ASN A1082 22.954 12.004−1.906 1.00 17.23 N ATOM 618 CA ASN A1082 23.266 10.615 −2.299 1.0018.16 C ATOM 619 CB ASN A1082 22.169 10.064 −3.227 1.00 19.47 C ATOM 620CG ASN A1082 20.853 9.800 −2.496 1.00 20.37 C ATOM 621 OD1 ASN A108220.701 8.793 −1.806 1.00 23.12 O ATOM 622 ND2 ASN A1082 19.908 10.709−2.637 1.00 21.16 N ATOM 623 C ASN A1082 24.633 10.540 −3.004 1.00 18.65C ATOM 624 O ASN A1082 24.894 11.311 −3.936 1.00 18.53 O ATOM 625 N ASNA1083 25.501 9.621 −2.567 1.00 18.47 N ATOM 626 CA ASN A1083 26.8409.496 −3.160 1.00 19.58 C ATOM 627 CB ASN A1083 27.823 8.831 −2.172 1.0019.14 C ATOM 628 CG ASN A1083 27.525 7.354 −1.898 1.00 19.47 C ATOM 629OD1 ASN A1083 28.000 6.806 −0.896 1.00 21.52 O ATOM 630 ND2 ASN A108326.774 6.705 −2.778 1.00 18.08 N ATOM 631 C ASN A1083 26.879 8.801−4.522 1.00 21.02 C ATOM 632 O ASN A1083 25.835 8.408 −5.053 1.00 20.46O ATOM 633 N GLU A1084 28.073 8.655 −5.095 1.00 22.56 N ATOM 634 CA GLUA1084 28.183 8.048 −6.422 1.00 25.48 C ATOM 635 CB GLU A1084 29.6068.243 −6.993 1.00 26.01 C ATOM 636 CG GLU A1084 30.704 7.346 −6.452 1.0027.48 C ATOM 637 CD GLU A1084 32.055 7.621 −7.127 1.00 28.81 C ATOM 638OE1 GLU A1084 32.087 7.807 −8.365 1.00 28.44 O ATOM 639 OE2 GLU A108433.085 7.644 −6.424 1.00 29.66 O ATOM 640 C GLU A1084 27.747 6.583−6.523 1.00 26.10 C ATOM 641 O GLU A1084 27.675 6.030 −7.618 1.00 26.96O ATOM 642 N ARG A1085 27.446 5.958 −5.390 1.00 26.87 N ATOM 643 CA ARGA1085 26.976 4.571 −5.381 1.00 27.01 C ATOM 644 CB ARG A1085 27.6973.761 −4.302 1.00 29.89 C ATOM 645 CG ARG A1085 29.210 3.670 −4.479 1.0033.27 C ATOM 646 CD ARG A1085 29.603 2.687 −5.570 1.00 35.91 C ATOM 647NE ARG A1085 31.041 2.724 −5.834 1.00 37.82 N ATOM 648 CZ ARG A108531.696 1.814 −6.549 1.00 39.02 C ATOM 649 NH1 ARG A1085 33.005 1.929−6.739 1.00 39.21 N ATOM 650 NH2 ARG A1085 31.043 0.782 −7.067 1.0039.98 N ATOM 651 C ARG A1085 25.467 4.573 −5.097 1.00 26.06 C ATOM 652 OARG A1085 24.830 3.515 −5.033 1.00 26.15 O ATOM 653 N GLY A1086 24.9115.768 −4.907 1.00 24.38 N ATOM 654 CA GLY A1086 23.485 5.910 −4.649 1.0022.84 C ATOM 655 C GLY A1086 22.989 5.874 −3.207 1.00 21.70 C ATOM 656 OGLY A1086 21.780 5.910 −2.980 1.00 21.52 O ATOM 657 N ALA A1087 23.8965.813 −2.234 1.00 20.27 N ATOM 658 CA ALA A1087 23.506 5.757 −0.819 1.0019.12 C ATOM 659 CB ALA A1087 24.452 4.825 −0.065 1.00 19.31 C ATOM 660C ALA A1087 23.468 7.126 −0.123 1.00 18.28 C ATOM 661 O ALA A1087 24.2938.001 −0.400 1.00 17.46 O ATOM 662 N PRO A1088 22.511 7.322 0.807 1.0017.16 N ATOM 663 CD PRO A1088 21.424 6.400 1.186 1.00 17.79 C ATOM 664CA PRO A1088 22.398 8.598 1.529 1.00 16.21 C ATOM 665 CB PRO A108821.053 8.469 2.263 1.00 16.47 C ATOM 666 CG PRO A1088 20.938 6.995 2.5071.00 17.39 C ATOM 667 C PRO A1088 23.579 8.828 2.481 1.00 15.55 C ATOM668 O PRO A1088 24.084 7.876 3.082 1.00 14.47 O ATOM 669 N TYR A108924.018 10.085 2.597 1.00 14.68 N ATOM 670 CA TYR A1089 25.148 10.4533.466 1.00 15.17 C ATOM 671 CB TYR A1089 26.478 10.205 2.728 1.00 15.96C ATOM 672 CG TYR A1089 26.834 11.280 1.707 1.00 17.14 C ATOM 673 CD1TYR A1089 27.815 12.240 1.980 1.00 17.14 C ATOM 674 CE1 TYR A1089 28.13613.243 1.042 1.00 17.71 C ATOM 675 CD2 TYR A1089 26.180 11.345 0.4761.00 17.70 C ATOM 676 CE2 TYR A1089 26.490 12.342 −0.470 1.00 18.23 CATOM 677 CZ TYR A1089 27.467 13.286 −0.180 1.00 18.79 C ATOM 678 OH TYRA1089 27.769 14.272 −1.110 1.00 18.83 O ATOM 679 C TYR A1089 25.06811.931 3.886 1.00 15.23 C ATOM 680 O TYR A1089 24.480 12.749 3.172 1.0014.55 O ATOM 681 N PHE A1090 25.664 12.276 5.030 1.00 15.03 N ATOM 682CA PHE A1090 25.646 13.668 5.502 1.00 16.07 C ATOM 683 CB PHE A109025.891 13.743 7.023 1.00 15.87 C ATOM 684 CG PHE A1090 24.662 13.4697.864 1.00 15.54 C ATOM 685 CD1 PHE A1090 24.359 12.176 8.287 1.00 14.81C ATOM 686 CD2 PHE A1090 23.798 14.512 8.213 1.00 15.28 C ATOM 687 CE1PHE A1090 23.207 11.920 9.048 1.00 15.40 C ATOM 688 CE2 PHE A1090 22.64314.272 8.973 1.00 16.17 C ATOM 689 CZ PHE A1090 22.347 12.971 9.390 1.0015.25 C ATOM 690 C PHE A1090 26.694 14.553 4.800 1.00 16.94 C ATOM 691 OPHE A1090 27.898 14.378 5.005 1.00 15.67 O ATOM 692 N SER A1091 26.23315.499 3.983 1.00 18.05 N ATOM 693 CA SER A1091 27.135 16.421 3.285 1.0020.04 C ATOM 694 CB SER A1091 26.528 16.864 1.949 1.00 20.26 C ATOM 695OG SER A1091 25.196 17.305 2.106 1.00 21.03 O ATOM 696 C SER A109127.456 17.653 4.143 1.00 20.79 C ATOM 697 O SER A1091 28.445 18.3493.890 1.00 21.71 O ATOM 698 N GLN A1092 26.606 17.930 5.133 1.00 20.94 NATOM 699 CA GLN A1092 26.810 19.049 6.062 1.00 21.39 C ATOM 700 CB GLNA1092 25.958 20.265 5.665 1.00 23.27 C ATOM 701 CG GLN A1092 26.26720.898 4.305 1.00 25.76 C ATOM 702 CD GLN A1092 27.623 21.589 4.244 1.0027.71 C ATOM 703 OE1 GLN A1092 28.044 22.248 5.197 1.00 29.37 O ATOM 704NE2 GLN A1092 28.301 21.461 3.106 1.00 28.25 N ATOM 705 C GLN A109226.416 18.619 7.489 1.00 20.95 C ATOM 706 O GLN A1092 25.340 18.0647.689 1.00 20.12 O ATOM 707 N ALA A1093 27.290 18.868 8.466 1.00 20.33 NATOM 708 CA ALA A1093 27.030 18.533 9.874 1.00 20.84 C ATOM 709 CB ALAA1093 26.874 17.013 10.046 1.00 20.16 C ATOM 710 C ALA A1093 28.17919.041 10.757 1.00 21.48 C ATOM 711 O ALA A1093 29.319 19.128 10.3041.00 21.44 O ATOM 712 N PRO A1094 27.890 19.389 12.027 1.00 22.28 N ATOM713 CD PRO A1094 26.539 19.598 12.585 1.00 22.57 C ATOM 714 CA PRO A109428.921 19.887 12.954 1.00 22.63 C ATOM 715 CB PRO A1094 28.125 20.80313.876 1.00 22.88 C ATOM 716 CG PRO A1094 26.828 20.043 14.020 1.0023.37 C ATOM 717 C PRO A1094 29.678 18.791 13.731 1.00 23.05 C ATOM 718O PRO A1094 29.571 18.700 14.959 1.00 23.97 O ATOM 719 N PHE A109530.446 17.976 13.009 1.00 22.89 N ATOM 720 CA PHE A1095 31.232 16.88313.590 1.00 22.99 C ATOM 721 CB PHE A1095 30.341 15.639 13.767 1.0022.67 C ATOM 722 CG PHE A1095 31.067 14.436 14.307 1.00 22.55 C ATOM 723CD1 PHE A1095 31.374 13.360 13.474 1.00 22.34 C ATOM 724 CD2 PHE A109531.462 14.385 15.641 1.00 22.13 C ATOM 725 CE1 PHE A1095 32.068 12.25013.963 1.00 22.27 C ATOM 726 CE2 PHE A1095 32.156 13.281 16.143 1.0022.71 C ATOM 727 CZ PHE A1095 32.461 12.209 15.300 1.00 22.51 C ATOM 728C PHE A1095 32.406 16.592 12.639 1.00 23.22 C ATOM 729 O PHE A109532.221 16.574 11.426 1.00 23.38 O ATOM 730 N SER A1096 33.602 16.35313.183 1.00 23.37 N ATOM 731 CA SER A1096 34.792 16.122 12.347 1.0023.62 C ATOM 732 CB SER A1096 35.993 16.858 12.955 1.00 24.11 C ATOM 733OG SER A1096 36.331 16.317 14.223 1.00 26.37 O ATOM 734 C SER A109635.233 14.691 12.000 1.00 23.23 C ATOM 735 O SER A1096 36.094 14.51011.125 1.00 22.88 O ATOM 736 N GLY A1097 34.670 13.686 12.669 1.00 22.73N ATOM 737 CA GLY A1097 35.043 12.304 12.391 1.00 21.96 C ATOM 738 C GLYA1097 34.138 11.589 11.393 1.00 21.41 C ATOM 739 O GLY A1097 33.51812.232 10.555 1.00 21.73 O ATOM 740 N LYS A1098 34.066 10.259 11.4791.00 20.96 N ATOM 741 CA LYS A1098 33.228 9.456 10.578 1.00 20.77 C ATOM742 CB LYS A1098 33.822 8.052 10.409 1.00 22.35 C ATOM 743 CG LYS A109835.205 8.017 9.774 1.00 25.18 C ATOM 744 CD LYS A1098 35.630 6.587 9.4491.00 26.26 C ATOM 745 CE LYS A1098 36.996 6.553 8.772 1.00 28.39 C ATOM746 NZ LYS A1098 37.332 5.194 8.258 1.00 28.94 N ATOM 747 C LYS A109831.770 9.313 11.046 1.00 19.74 C ATOM 748 O LYS A1098 31.517 9.06412.224 1.00 19.90 O ATOM 749 N ILE A1099 30.826 9.461 10.113 1.00 18.27N ATOM 750 CA ILE A1099 29.393 9.340 10.400 1.00 17.38 C ATOM 751 CB ILEA1099 28.622 10.638 9.997 1.00 17.39 C ATOM 752 CG2 ILE A1099 27.12410.465 10.284 1.00 16.62 C ATOM 753 CG1 ILE A1099 29.171 11.849 10.7611.00 15.42 C ATOM 754 CD1 ILE A1099 28.790 13.196 10.165 1.00 15.80 CATOM 755 C ILE A1099 28.777 8.164 9.607 1.00 17.23 C ATOM 756 O ILEA1099 28.697 8.226 8.381 1.00 18.55 O ATOM 757 N TRP A1100 28.356 7.10210.298 1.00 16.06 N ATOM 758 CA TRP A1100 27.733 5.939 9.641 1.00 15.73C ATOM 759 CB TRP A1100 28.163 4.638 10.347 1.00 15.81 C ATOM 760 CG TRPA1100 29.665 4.374 10.328 1.00 16.55 C ATOM 761 CD2 TRP A1100 30.4153.750 9.274 1.00 16.48 C ATOM 762 CE2 TRP A1100 31.774 3.736 9.676 1.0017.61 C ATOM 763 CE3 TRP A1100 30.071 3.199 8.030 1.00 17.03 C ATOM 764CD1 TRP A1100 30.575 4.704 11.300 1.00 17.00 C ATOM 765 NE1 TRP A110031.844 4.322 10.916 1.00 16.91 N ATOM 766 CZ2 TRP A1100 32.792 3.1918.873 1.00 17.99 C ATOM 767 CZ3 TRP A1100 31.083 2.654 7.230 1.00 18.05C ATOM 768 CH2 TRP A1100 32.430 2.656 7.659 1.00 17.40 C ATOM 769 C TRPA1100 26.190 6.079 9.705 1.00 15.39 C ATOM 770 O TRP A1100 25.638 6.16010.801 1.00 15.11 O ATOM 771 N LEU A1101 25.517 6.100 8.545 1.00 14.54 NATOM 772 CA LEU A1101 24.045 6.260 8.448 1.00 14.10 C ATOM 773 CB LEUA1101 23.705 7.658 7.883 1.00 14.83 C ATOM 774 CG LEU A1101 22.267 7.8937.366 1.00 15.12 C ATOM 775 CD1 LEU A1101 21.330 8.116 8.541 1.00 15.77C ATOM 776 CD2 LEU A1101 22.216 9.105 6.427 1.00 15.58 C ATOM 777 C LEUA1101 23.318 5.214 7.576 1.00 13.98 C ATOM 778 O LEU A1101 23.847 4.7896.537 1.00 13.24 O ATOM 779 N SER A1102 22.109 4.808 7.996 1.00 13.49 NATOM 780 CA SER A1102 21.278 3.857 7.226 1.00 14.16 C ATOM 781 CB SERA1102 21.525 2.411 7.683 1.00 14.32 C ATOM 782 OG SER A1102 20.947 1.4716.781 1.00 14.30 O ATOM 783 C SER A1102 19.777 4.190 7.363 1.00 14.45 CATOM 784 O SER A1102 19.311 4.519 8.464 1.00 13.54 O ATOM 785 N ILEA1103 19.029 4.089 6.254 1.00 14.69 N ATOM 786 CA ILE A1103 17.575 4.3876.231 1.00 15.31 C ATOM 787 CB ILE A1103 17.282 5.709 5.454 1.00 15.58 CATOM 788 CG2 ILE A1103 15.783 6.027 5.508 1.00 15.76 C ATOM 789 CG1 ILEA1103 18.085 6.875 6.041 1.00 15.76 C ATOM 790 CD1 ILE A1103 17.8388.216 5.317 1.00 17.30 C ATOM 791 C ILE A1103 16.766 3.263 5.541 1.0015.22 C ATOM 792 O ILE A1103 17.249 2.668 4.575 1.00 16.46 O ATOM 793 NSER A1104 15.550 2.977 6.023 1.00 15.94 N ATOM 794 CA SER A1104 14.6861.926 5.429 1.00 17.08 C ATOM 795 CB SER A1104 14.993 0.564 6.085 1.0017.67 C ATOM 796 OG SER A1104 14.251 −0.486 5.476 1.00 17.18 O ATOM 797C SER A1104 13.174 2.248 5.574 1.00 17.46 C ATOM 798 O SER A1104 12.7842.982 6.483 1.00 16.57 O ATOM 799 N HIS A1105 12.323 1.699 4.698 1.0018.34 N ATOM 800 CA HIS A1105 10.877 1.989 4.776 1.00 19.13 C ATOM 801CB HIS A1105 10.572 3.300 4.041 1.00 20.61 C ATOM 802 CG HIS A110510.702 3.188 2.551 1.00 21.51 C ATOM 803 CD2 HIS A1105 9.799 2.840 1.6011.00 22.68 C ATOM 804 ND1 HIS A1105 11.906 3.333 1.896 1.00 23.14 N ATOM805 CE1 HIS A1105 11.742 3.075 0.610 1.00 23.36 C ATOM 806 NE2 HIS A110510.473 2.772 0.405 1.00 22.97 N ATOM 807 C HIS A1105 9.918 0.933 4.1921.00 19.69 C ATOM 808 O HIS A1105 10.324 0.073 3.405 1.00 19.77 O ATOM809 N THR A1106 8.640 1.034 4.577 1.00 20.07 N ATOM 810 CA THR A11067.564 0.171 4.056 1.00 20.65 C ATOM 811 CB THR A1106 6.941 −0.769 5.1311.00 20.02 C ATOM 812 OG1 THR A1106 6.198 0.004 6.085 1.00 19.30 O ATOM813 CG2 THR A1106 8.029 −1.578 5.852 1.00 19.90 C ATOM 814 C THR A11066.470 1.143 3.587 1.00 22.48 C ATOM 815 O THR A1106 6.720 2.347 3.4761.00 21.87 O ATOM 816 N ASP A1107 5.262 0.652 3.315 1.00 23.59 N ATOM817 CA ASP A1107 4.214 1.569 2.875 1.00 25.20 C ATOM 818 CB ASP A11073.146 0.831 2.052 1.00 27.87 C ATOM 819 CG ASP A1107 2.302 −0.116 2.8861.00 29.94 C ATOM 820 OD1 ASP A1107 1.331 −0.672 2.332 1.00 32.47 O ATOM821 OD2 ASP A1107 2.601 −0.314 4.086 1.00 32.30 O ATOM 822 C ASP A11073.549 2.322 4.027 1.00 25.08 C ATOM 823 O ASP A1107 2.673 3.156 3.7911.00 25.52 O ATOM 824 N GLN A1108 3.965 2.042 5.264 1.00 24.18 N ATOM825 CA GLN A1108 3.380 2.703 6.435 1.00 23.78 C ATOM 826 CB GLN A11082.533 1.715 7.251 1.00 25.19 C ATOM 827 CG GLN A1108 1.283 1.211 6.5501.00 28.60 C ATOM 828 CD GLN A1108 0.375 0.426 7.479 1.00 30.45 C ATOM829 OE1 GLN A1108 0.768 −0.606 8.026 1.00 31.65 O ATOM 830 NE2 GLN A1108−0.847 0.918 7.670 1.00 31.23 N ATOM 831 C GLN A1108 4.361 3.391 7.3901.00 22.77 C ATOM 832 O GLN A1108 3.966 4.334 8.081 1.00 22.34 O ATOM833 N PHE A1109 5.616 2.926 7.441 1.00 21.34 N ATOM 834 CA PHE A11096.633 3.513 8.342 1.00 20.67 C ATOM 835 CB PHE A1109 6.888 2.605 9.5671.00 21.50 C ATOM 836 CG PHE A1109 5.654 2.213 10.328 1.00 22.53 C ATOM837 CD1 PHE A1109 4.947 1.059 9.989 1.00 23.72 C ATOM 838 CD2 PHE A11095.212 2.978 11.403 1.00 23.05 C ATOM 839 CE1 PHE A1109 3.816 0.67310.715 1.00 24.14 C ATOM 840 CE2 PHE A1109 4.082 2.601 12.135 1.00 24.05C ATOM 841 CZ PHE A1109 3.383 1.445 11.789 1.00 23.64 C ATOM 842 C PHEA1109 8.015 3.755 7.705 1.00 19.29 C ATOM 843 O PHE A1109 8.333 3.1996.654 1.00 19.32 O ATOM 844 N VAL A1110 8.830 4.582 8.368 1.00 18.27 NATOM 845 CA VAL A1110 10.218 4.864 7.955 1.00 16.90 C ATOM 846 CB VALA1110 10.368 6.279 7.299 1.00 17.79 C ATOM 847 CG1 VAL A1110 10.1267.377 8.325 1.00 17.09 C ATOM 848 CG2 VAL A1110 11.754 6.428 6.681 1.0017.98 C ATOM 849 C VAL A1110 11.100 4.796 9.224 1.00 16.47 C ATOM 850 OVAL A1110 10.655 5.214 10.300 1.00 15.21 O ATOM 851 N THR A1111 12.3234.260 9.097 1.00 15.44 N ATOM 852 CA THR A1111 13.271 4.126 10.225 1.0016.10 C ATOM 853 CB THR A1111 13.369 2.646 10.736 1.00 16.89 C ATOM 854OG1 THR A1111 13.775 1.775 9.667 1.00 18.14 O ATOM 855 CG2 THR A111112.038 2.180 11.274 1.00 18.11 C ATOM 856 C THR A1111 14.692 4.582 9.8601.00 15.27 C ATOM 857 O THR A1111 15.082 4.502 8.690 1.00 14.78 O ATOM858 N ALA A1112 15.462 5.041 10.858 1.00 14.23 N ATOM 859 CA ALA A111216.845 5.505 10.639 1.00 13.59 C ATOM 860 CB ALA A1112 16.855 7.00110.293 1.00 12.71 C ATOM 861 C ALA A1112 17.764 5.255 11.843 1.00 12.99C ATOM 862 O ALA A1112 17.310 5.303 12.993 1.00 12.81 O ATOM 863 N SERA1113 19.055 5.032 11.570 1.00 12.47 N ATOM 864 CA SER A1113 20.0644.761 12.610 1.00 13.04 C ATOM 865 CB SER A1113 20.256 3.238 12.736 1.0013.53 C ATOM 866 OG SER A1113 21.244 2.893 13.698 1.00 13.09 O ATOM 867C SER A1113 21.427 5.444 12.318 1.00 13.78 C ATOM 868 O SER A1113 21.9015.419 11.180 1.00 13.46 O ATOM 869 N VAL A1114 22.048 6.039 13.348 1.0013.44 N ATOM 870 CA VAL A1114 23.349 6.735 13.208 1.00 12.85 C ATOM 871CB VAL A1114 23.151 8.288 13.286 1.00 12.88 C ATOM 872 CG1 VAL A111424.496 9.005 13.384 1.00 12.82 C ATOM 873 CG2 VAL A1114 22.384 8.79412.056 1.00 13.36 C ATOM 874 C VAL A1114 24.393 6.328 14.278 1.00 12.70C ATOM 875 O VAL A1114 24.045 6.140 15.444 1.00 12.48 O ATOM 876 N ILEA1115 25.662 6.183 13.873 1.00 13.61 N ATOM 877 CA ILE A1115 26.7655.846 14.800 1.00 13.97 C ATOM 878 CB ILE A1115 27.291 4.399 14.621 1.0014.70 C ATOM 879 CG2 ILE A1115 28.393 4.124 15.653 1.00 15.55 C ATOM 880CG1 ILE A1115 26.163 3.377 14.800 1.00 14.56 C ATOM 881 CD1 ILE A111526.580 1.948 14.433 1.00 14.04 C ATOM 882 C ILE A1115 27.940 6.78614.502 1.00 15.39 C ATOM 883 O ILE A1115 28.372 6.879 13.348 1.00 14.30O ATOM 884 N LEU A1116 28.456 7.465 15.537 1.00 15.93 N ATOM 885 CA LEUA1116 29.574 8.412 15.397 1.00 16.40 C ATOM 886 CB LEU A1116 29.3009.680 16.235 1.00 16.45 C ATOM 887 CG LEU A1116 27.972 10.439 16.0511.00 15.86 C ATOM 888 CD1 LEU A1116 27.935 11.642 16.994 1.00 16.47 CATOM 889 CD2 LEU A1116 27.816 10.888 14.601 1.00 16.74 C ATOM 890 C LEUA1116 30.906 7.778 15.839 1.00 17.18 C ATOM 891 O LEU A1116 30.973 7.12516.880 1.00 15.82 O ATOM 892 N GLU A1117 31.970 8.002 15.064 1.00 18.58N ATOM 893 CA GLU A1117 33.278 7.414 15.362 1.00 21.21 C ATOM 894 CB GLUA1117 33.404 6.068 14.615 1.00 21.29 C ATOM 895 CG GLU A1117 34.7935.403 14.659 1.00 21.49 C ATOM 896 CD GLU A1117 34.930 4.238 13.675 1.0021.22 C ATOM 897 OE1 GLU A1117 34.538 4.390 12.500 1.00 20.57 O ATOM 898OE2 GLU A1117 35.446 3.166 14.064 1.00 22.68 O ATOM 899 C GLU A111734.487 8.290 15.001 1.00 23.59 C ATOM 900 O GLU A1117 34.440 9.10814.083 1.00 22.02 O ATOM 901 N GLU A1118 35.576 8.115 15.740 1.00 27.34N ATOM 902 CA GLU A1118 36.801 8.839 15.429 1.00 31.25 C ATOM 903 CB GLUA1118 36.859 10.184 16.157 1.00 33.00 C ATOM 904 CG GLU A1118 36.74710.131 17.651 1.00 35.45 C ATOM 905 CD GLU A1118 37.042 11.480 18.2691.00 37.44 C ATOM 906 OE1 GLU A1118 36.389 12.470 17.874 1.00 38.60 OATOM 907 OE2 GLU A1118 37.932 11.551 19.145 1.00 39.01 O ATOM 908 C GLUA1118 38.005 7.964 15.764 1.00 33.04 C ATOM 909 O GLU A1118 38.074 7.35816.835 1.00 33.37 O ATOM 910 N ASN A1119 38.928 7.875 14.809 1.00 34.80N ATOM 911 CA ASN A1119 40.132 7.063 14.945 1.00 36.61 C ATOM 912 CB ASNA1119 40.203 6.015 13.823 1.00 37.32 C ATOM 913 CG ASN A1119 38.8625.356 13.537 1.00 38.38 C ATOM 914 OD1 ASN A1119 38.258 4.731 14.4091.00 39.30 O ATOM 915 ND2 ASN A1119 38.393 5.492 12.302 1.00 38.79 NATOM 916 C ASN A1119 41.354 7.972 14.845 1.00 37.29 C ATOM 917 O ASNA1119 42.132 7.795 13.885 1.00 37.98 O ATOM 918 OXT ASN A1119 41.5138.857 15.710 1.00 38.37 O TER 919 ASN A1119 ATOM 920 CB MET B2003 37.510−3.957 21.175 1.00 28.67 C ATOM 921 CG MET B2003 37.230 −5.443 21.0921.00 31.61 C ATOM 922 SD MET B2003 38.381 −6.420 22.089 1.00 36.00 SATOM 923 CE MET B2003 37.478 −6.538 23.632 1.00 34.64 C ATOM 924 C METB2003 35.111 −3.318 20.851 1.00 24.52 C ATOM 925 O MET B2003 34.821−3.223 22.044 1.00 23.78 O ATOM 926 N MET B2003 36.911 −1.645 20.5361.00 26.75 N ATOM 927 CA MET B2003 36.543 −3.080 20.373 1.00 26.43 CATOM 928 N ILE B2004 34.220 −3.611 19.907 1.00 23.33 N ATOM 929 CA ILEB2004 32.814 −3.877 20.214 1.00 21.77 C ATOM 930 CB ILE B2004 31.948−3.818 18.923 1.00 22.25 C ATOM 931 CG2 ILE B2004 30.528 −4.317 19.2141.00 21.40 C ATOM 932 CG1 ILE B2004 31.936 −2.387 18.370 1.00 22.04 CATOM 933 CD1 ILE B2004 31.248 −2.242 17.013 1.00 23.31 C ATOM 934 C ILEB2004 32.688 −5.268 20.837 1.00 21.10 C ATOM 935 O ILE B2004 33.423−6.190 20.463 1.00 21.53 O ATOM 936 N VAL B2005 31.774 −5.423 21.7931.00 19.59 N ATOM 937 CA VAL B2005 31.577 −6.725 22.423 1.00 18.29 CATOM 938 CB VAL B2005 32.240 −6.783 23.834 1.00 18.82 C ATOM 939 CG1 VALB2005 33.741 −6.518 23.712 1.00 18.55 C ATOM 940 CG2 VAL B2005 31.596−5.776 24.778 1.00 19.42 C ATOM 941 C VAL B2005 30.108 −7.189 22.5201.00 17.17 C ATOM 942 O VAL B2005 29.827 −8.180 23.193 1.00 16.88 O ATOM943 N GLY B2006 29.190 −6.493 21.838 1.00 15.24 N ATOM 944 CA GLY B200627.776 −6.881 21.849 1.00 14.41 C ATOM 945 C GLY B2006 26.800 −5.89921.191 1.00 13.76 C ATOM 946 O GLY B2006 27.067 −4.703 21.177 1.00 12.82O ATOM 947 N HIS B2007 25.667 −6.388 20.664 1.00 13.79 N ATOM 948 CA HISB2007 24.656 −5.521 20.015 1.00 13.97 C ATOM 949 CB HIS B2007 25.046−5.296 18.534 1.00 13.17 C ATOM 950 CG HIS B2007 24.110 −4.400 17.7671.00 13.29 C ATOM 951 CD2 HIS B2007 23.648 −4.481 16.494 1.00 13.60 CATOM 952 ND1 HIS B2007 23.602 −3.224 18.281 1.00 14.70 N ATOM 953 CE1HIS B2007 22.871 −2.619 17.357 1.00 15.43 C ATOM 954 NE2 HIS B200722.884 −3.360 16.262 1.00 13.92 N ATOM 955 C HIS B2007 23.227 −6.10820.104 1.00 13.36 C ATOM 956 O HIS B2007 23.024 −7.293 19.817 1.00 13.30O ATOM 957 N GLY B2008 22.249 −5.286 20.504 1.00 13.56 N ATOM 958 CA GLYB2008 20.870 −5.758 20.603 1.00 13.42 C ATOM 959 C GLY B2008 19.760−4.724 20.407 1.00 13.33 C ATOM 960 O GLY B2008 19.921 −3.566 20.7861.00 13.08 O ATOM 961 N ILE B2009 18.630 −5.143 19.827 1.00 13.48 N ATOM962 CA ILE B2009 17.476 −4.253 19.601 1.00 13.81 C ATOM 963 CB ILE B200917.327 −3.864 18.086 1.00 14.27 C ATOM 964 CG2 ILE B2009 18.651 −3.27617.549 1.00 14.33 C ATOM 965 CG1 ILE B2009 16.931 −5.091 17.257 1.0014.49 C ATOM 966 CD1 ILE B2009 16.666 −4.783 15.777 1.00 15.47 C ATOM967 C ILE B2009 16.155 −4.916 20.066 1.00 14.94 C ATOM 968 O ILE B200916.090 −6.145 20.190 1.00 14.51 O ATOM 969 N ASP B2010 15.115 −4.11120.318 1.00 15.66 N ATOM 970 CA ASP B2010 13.806 −4.644 20.746 1.0017.47 C ATOM 971 CB ASP B2010 13.820 −4.974 22.250 1.00 18.72 C ATOM 972CG ASP B2010 12.474 −5.527 22.757 1.00 19.74 C ATOM 973 OD1 ASP B201011.670 −4.747 23.311 1.00 21.08 O ATOM 974 OD2 ASP B2010 12.214 −6.74022.593 1.00 19.62 O ATOM 975 C ASP B2010 12.623 −3.709 20.447 1.00 18.58C ATOM 976 O ASP B2010 12.769 −2.483 20.472 1.00 17.47 O ATOM 977 N ILEB2011 11.465 −4.304 20.148 1.00 19.97 N ATOM 978 CA ILE B2011 10.224−3.558 19.874 1.00 22.59 C ATOM 979 CB ILE B2011 9.666 −3.817 18.4591.00 23.44 C ATOM 980 CG2 ILE B2011 8.532 −2.831 18.167 1.00 24.17 CATOM 981 CG1 ILE B2011 10.752 −3.688 17.411 1.00 23.83 C ATOM 982 CD1ILE B2011 10.368 −4.350 16.110 1.00 24.58 C ATOM 983 C ILE B2011 9.134−4.066 20.833 1.00 23.70 C ATOM 984 O ILE B2011 9.039 −5.271 21.078 1.0023.87 O ATOM 985 N GLU B2012 8.305 −3.166 21.359 1.00 24.36 N ATOM 986CA GLU B2012 7.232 −3.569 22.270 1.00 25.44 C ATOM 987 CB GLU B20127.626 −3.297 23.723 1.00 26.83 C ATOM 988 CG GLU B2012 6.659 −3.89624.741 1.00 29.96 C ATOM 989 CD GLU B2012 6.806 −5.408 24.892 1.00 32.18C ATOM 990 OE1 GLU B2012 7.094 −6.098 23.888 1.00 33.01 O ATOM 991 OE2GLU B2012 6.617 −5.908 26.024 1.00 33.41 O ATOM 992 C GLU B2012 5.915−2.848 21.952 1.00 25.77 C ATOM 993 O GLU B2012 5.911 −1.677 21.585 1.0024.25 O ATOM 994 N GLU B2013 4.800 −3.563 22.089 1.00 26.07 N ATOM 995CA GLU B2013 3.483 −2.997 21.806 1.00 26.79 C ATOM 996 CB GLU B20132.546 −4.097 21.294 1.00 27.06 C ATOM 997 CG GLU B2013 3.025 −4.77720.014 1.00 27.29 C ATOM 998 CD GLU B2013 2.147 −5.943 19.607 0.05 27.19C ATOM 999 OE1 GLU B2013 0.920 −5.750 19.479 0.05 27.19 O ATOM 1000 OE2GLU B2013 2.684 −7.054 19.413 0.05 27.19 O ATOM 1001 C GLU B2013 2.895−2.358 23.061 1.00 27.09 C ATOM 1002 O GLU B2013 2.816 −2.998 24.1131.00 27.20 O ATOM 1003 N LEU B2014 2.489 −1.096 22.952 1.00 27.74 N ATOM1004 CA LEU B2014 1.915 −0.383 24.088 1.00 28.99 C ATOM 1005 CB LEUB2014 1.448 1.015 23.666 1.00 29.85 C ATOM 1006 CG LEU B2014 2.499 2.06423.293 1.00 30.49 C ATOM 1007 CD1 LEU B2014 1.802 3.353 22.863 1.0031.36 C ATOM 1008 CD2 LEU B2014 3.408 2.332 24.477 1.00 30.66 C ATOM1009 C LEU B2014 0.742 −1.144 24.705 1.00 29.62 C ATOM 1010 O LEU B20140.614 −1.209 25.924 1.00 28.92 O ATOM 1011 N ALA B2015 −0.103 −1.72323.855 1.00 30.68 N ATOM 1012 CA ALA B2015 −1.273 −2.468 24.312 1.0031.89 C ATOM 1013 CB ALA B2015 −2.062 −2.992 23.106 1.00 31.63 C ATOM1014 C ALA B2015 −0.942 −3.624 25.256 1.00 32.68 C ATOM 1015 O ALA B2015−1.705 −3.913 26.180 1.00 32.95 O ATOM 1016 N SER B2016 0.192 −4.28225.026 1.00 32.98 N ATOM 1017 CA SER B2016 0.599 −5.409 25.861 1.0033.69 C ATOM 1018 CB SER B2016 1.758 −6.157 25.205 1.00 34.30 C ATOM1019 OG SER B2016 1.360 −6.697 23.955 1.00 36.37 O ATOM 1020 C SER B20160.993 −4.981 27.271 1.00 33.62 C ATOM 1021 O SER B2016 0.707 −5.68028.242 1.00 33.30 O ATOM 1022 N ILE B2017 1.656 −3.835 27.384 1.00 33.85N ATOM 1023 CA ILE B2017 2.056 −3.339 28.694 1.00 34.29 C ATOM 1024 CBILE B2017 2.995 −2.115 28.571 1.00 34.08 C ATOM 1025 CG2 ILE B2017 3.350−1.588 29.958 1.00 33.83 C ATOM 1026 CG1 ILE B2017 4.264 −2.501 27.8001.00 33.75 C ATOM 1027 CD1 ILE B2017 5.080 −3.611 28.449 1.00 33.98 CATOM 1028 C ILE B2017 0.802 −2.932 29.474 1.00 35.14 C ATOM 1029 O ILEB2017 0.714 −3.143 30.683 1.00 34.67 O ATOM 1030 N GLU B2018 −0.172−2.362 28.770 1.00 36.36 N ATOM 1031 CA GLU B2018 −1.414 −1.925 29.4021.00 37.92 C ATOM 1032 CB GLU B2018 −2.292 −1.189 28.386 1.00 38.65 CATOM 1033 CG GLU B2018 −1.548 −0.122 27.599 1.00 40.03 C ATOM 1034 CDGLU B2018 −2.462 0.705 26.716 1.00 41.09 C ATOM 1035 OE1 GLU B2018−3.463 0.148 26.216 1.00 41.60 O ATOM 1036 OE2 GLU B2018 −2.172 1.90726.510 1.00 41.15 O ATOM 1037 C GLU B2018 −2.189 −3.093 30.011 1.0038.32 C ATOM 1038 O GLU B2018 −2.697 −2.993 31.129 1.00 39.05 O ATOM1039 N SER B2019 −2.281 −4.198 29.278 1.00 38.71 N ATOM 1040 CA SERB2019 −2.989 −5.375 29.771 1.00 39.10 C ATOM 1041 CB SER B2019 −2.996−6.476 28.709 1.00 39.02 C ATOM 1042 OG SER B2019 −3.734 −6.082 27.5681.00 39.39 O ATOM 1043 C SER B2019 −2.332 −5.903 31.044 1.00 39.56 CATOM 1044 O SER B2019 −3.013 −6.228 32.016 1.00 39.07 O ATOM 1045 N ALAB2020 −1.004 −5.983 31.031 1.00 39.92 N ATOM 1046 CA ALA B2020 −0.253−6.471 32.182 1.00 40.75 C ATOM 1047 CB ALA B2020 1.240 −6.474 31.8661.00 39.96 C ATOM 1048 C ALA B2020 −0.531 −5.614 33.415 1.00 41.51 CATOM 1049 O ALA B2020 −0.584 −6.122 34.535 1.00 41.34 O ATOM 1050 N VALB2021 −0.704 −4.314 33.202 1.00 42.82 N ATOM 1051 CA VAL B2021 −0.985−3.390 34.295 1.00 44.39 C ATOM 1052 CB VAL B2021 −0.767 −1.922 33.8551.00 44.31 C ATOM 1053 CG1 VAL B2021 −1.303 −0.971 34.913 1.00 44.07 CATOM 1054 CG2 VAL B2021 0.718 −1.663 33.627 1.00 44.22 C ATOM 1055 C VALB2021 −2.424 −3.555 34.787 1.00 45.72 C ATOM 1056 O VAL B2021 −2.673−3.604 35.992 1.00 45.74 O ATOM 1057 N THR B2022 −3.365 −3.642 33.8511.00 47.27 N ATOM 1058 CA THR B2022 −4.776 −3.801 34.191 1.00 48.73 CATOM 1059 CB THR B2022 −5.661 −3.833 32.919 1.00 49.02 C ATOM 1060 OG1THR B2022 −5.482 −2.619 32.177 1.00 49.29 O ATOM 1061 CG2 THR B2022−7.134 −3.968 33.293 1.00 49.42 C ATOM 1062 C THR B2022 −4.988 −5.09334.977 1.00 49.61 C ATOM 1063 O THR B2022 −5.953 −5.225 35.733 1.0049.90 O ATOM 1064 N ARG B2023 −4.077 −6.043 34.794 1.00 50.61 N ATOM1065 CA ARG B2023 −4.152 −7.325 35.484 1.00 51.35 C ATOM 1066 CB ARGB2023 −3.028 −8.245 35.009 1.00 52.09 C ATOM 1067 CG ARG B2023 −3.416−9.710 34.907 1.00 53.02 C ATOM 1068 CD ARG B2023 −3.676 −10.103 33.4611.00 54.10 C ATOM 1069 NE ARG B2023 −2.492 −9.895 32.628 1.00 54.73 NATOM 1070 CZ ARG B2023 −2.419 −10.194 31.334 1.00 55.21 C ATOM 1071 NH1ARG B2023 −3.465 −10.720 30.710 1.00 55.43 N ATOM 1072 NH2 ARG B2023−1.296 −9.967 30.663 1.00 55.24 N ATOM 1073 C ARG B2023 −4.025 −7.09336.989 1.00 51.64 C ATOM 1074 O ARG B2023 −4.448 −7.924 37.794 1.0051.91 O ATOM 1075 N HIS B2024 −3.428 −5.960 37.354 1.00 51.80 N ATOM1076 CA HIS B2024 −3.242 −5.575 38.753 1.00 51.59 C ATOM 1077 CB HISB2024 −4.586 −5.645 39.491 1.00 52.56 C ATOM 1078 CG HIS B2024 −4.528−5.165 40.908 1.00 53.50 C ATOM 1079 CD2 HIS B2024 −4.815 −5.791 42.0741.00 53.85 C ATOM 1080 ND1 HIS B2024 −4.142 −3.886 41.245 1.00 53.73 NATOM 1081 CE1 HIS B2024 −4.195 −3.743 42.557 1.00 54.11 C ATOM 1082 NE2HIS B2024 −4.601 −4.885 43.084 1.00 54.34 N ATOM 1083 C HIS B2024 −2.207−6.427 39.490 1.00 50.92 C ATOM 1084 O HIS B2024 −1.802 −6.100 40.6071.00 51.09 O ATOM 1085 N GLU B2025 −1.777 −7.511 38.853 1.00 49.85 NATOM 1086 CA GLU B2025 −0.805 −8.436 39.429 1.00 48.60 C ATOM 1087 CBGLU B2025 −0.133 −9.231 38.309 1.00 49.70 C ATOM 1088 CG GLU B2025−1.109 −9.812 37.300 1.00 50.84 C ATOM 1089 CD GLU B2025 −0.430 −10.67636.255 1.00 51.43 C ATOM 1090 OE1 GLU B2025 0.084 −11.754 36.617 1.0052.08 O ATOM 1091 OE2 GLU B2025 −0.408 −10.276 35.073 1.00 51.96 O ATOM1092 C GLU B2025 0.274 −7.788 40.301 1.00 47.18 C ATOM 1093 O GLU B20250.636 −8.322 41.350 1.00 47.28 O ATOM 1094 N GLY B2026 0.779 −6.63839.864 1.00 45.23 N ATOM 1095 CA GLY B2026 1.832 −5.953 40.598 1.0042.17 C ATOM 1096 C GLY B2026 3.021 −5.830 39.663 1.00 39.71 C ATOM 1097O GLY B2026 4.185 −5.914 40.066 1.00 39.77 O ATOM 1098 N PHE B2027 2.695−5.632 38.392 1.00 37.19 N ATOM 1099 CA PHE B2027 3.667 −5.509 37.3151.00 34.55 C ATOM 1100 CB PHE B2027 2.922 −5.189 36.014 1.00 34.52 CATOM 1101 CG PHE B2027 3.752 −5.355 34.777 1.00 34.13 C ATOM 1102 CD1PHE B2027 4.207 −6.613 34.393 1.00 34.08 C ATOM 1103 CD2 PHE B2027 4.067−4.258 33.986 1.00 34.08 C ATOM 1104 CE1 PHE B2027 4.963 −6.776 33.2371.00 34.11 C ATOM 1105 CE2 PHE B2027 4.825 −4.409 32.824 1.00 34.27 CATOM 1106 CZ PHE B2027 5.274 −5.670 32.449 1.00 34.06 C ATOM 1107 C PHEB2027 4.755 −4.459 37.559 1.00 32.71 C ATOM 1108 O PHE B2027 5.933−4.794 37.676 1.00 31.86 O ATOM 1109 N ALA B2028 4.352 −3.192 37.6311.00 30.82 N ATOM 1110 CA ALA B2028 5.284 −2.082 37.831 1.00 29.20 CATOM 1111 CB ALA B2028 4.506 −0.787 38.047 1.00 29.12 C ATOM 1112 C ALAB2028 6.290 −2.269 38.966 1.00 28.66 C ATOM 1113 O ALA B2028 7.451−1.884 38.836 1.00 27.76 O ATOM 1114 N LYS B2029 5.846 −2.853 40.0751.00 27.74 N ATOM 1115 CA LYS B2029 6.718 −3.065 41.226 1.00 27.62 CATOM 1116 CB LYS B2029 5.899 −3.552 42.423 1.00 27.96 C ATOM 1117 CG LYSB2029 5.853 −2.569 43.584 1.00 28.74 C ATOM 1118 CD LYS B2029 7.247−2.299 44.131 0.05 28.50 C ATOM 1119 CE LYS B2029 7.204 −1.384 45.3430.05 28.61 C ATOM 1120 NZ LYS B2029 6.454 −1.997 46.474 0.05 28.56 NATOM 1121 C LYS B2029 7.864 −4.042 40.969 1.00 27.09 C ATOM 1122 O LYSB2029 8.937 −3.910 41.555 1.00 27.52 O ATOM 1123 N ARG B2030 7.642−5.022 40.099 1.00 25.99 N ATOM 1124 CA ARG B2030 8.682 −6.002 39.8031.00 24.71 C ATOM 1125 CB ARG B2030 8.048 −7.358 39.465 1.00 25.36 CATOM 1126 CG ARG B2030 7.303 −7.990 40.631 0.05 25.04 C ATOM 1127 CD ARGB2030 6.804 −9.384 40.291 0.05 25.09 C ATOM 1128 NE ARG B2030 6.143−10.015 41.430 0.05 25.02 N ATOM 1129 CZ ARG B2030 5.651 −11.249 41.4210.05 25.00 C ATOM 1130 NH1 ARG B2030 5.742 −11.996 40.329 0.05 24.97 NATOM 1131 NH2 ARG B2030 5.067 −11.739 42.506 0.05 24.97 N ATOM 1132 CARG B2030 9.616 −5.566 38.674 1.00 23.43 C ATOM 1133 O ARG B2030 10.763−6.008 38.613 1.00 22.95 O ATOM 1134 N VAL B2031 9.131 −4.688 37.7971.00 22.08 N ATOM 1135 CA VAL B2031 9.924 −4.202 36.665 1.00 20.91 CATOM 1136 CB VAL B2031 8.998 −3.878 35.447 1.00 21.66 C ATOM 1137 CG1VAL B2031 9.804 −3.269 34.307 1.00 21.12 C ATOM 1138 CG2 VAL B2031 8.311−5.152 34.961 1.00 21.59 C ATOM 1139 C VAL B2031 10.806 −2.971 36.9461.00 20.08 C ATOM 1140 O VAL B2031 11.891 −2.840 36.362 1.00 18.87 OATOM 1141 N LEU B2032 10.362 −2.096 37.851 1.00 18.43 N ATOM 1142 CA LEUB2032 11.093 −0.857 38.170 1.00 18.33 C ATOM 1143 CB LEU B2032 10.1230.333 38.094 1.00 18.11 C ATOM 1144 CG LEU B2032 9.264 0.562 36.836 1.0017.77 C ATOM 1145 CD1 LEU B2032 8.288 1.710 37.095 1.00 18.63 C ATOM1146 CD2 LEU B2032 10.141 0.893 35.642 1.00 18.26 C ATOM 1147 C LEUB2032 11.809 −0.804 39.537 1.00 18.11 C ATOM 1148 O LEU B2032 11.313−1.351 40.528 1.00 17.53 O ATOM 1149 N THR B2033 12.964 −0.133 39.5891.00 17.46 N ATOM 1150 CA THR B2033 13.707 0.022 40.848 1.00 17.07 CATOM 1151 CB THR B2033 15.178 0.466 40.617 1.00 17.19 C ATOM 1152 OG1THR B2033 15.199 1.760 39.996 1.00 17.05 O ATOM 1153 CG2 THR B203315.919 −0.544 39.733 1.00 15.96 C ATOM 1154 C THR B2033 13.010 1.10741.686 1.00 17.66 C ATOM 1155 O THR B2033 12.042 1.720 41.234 1.00 17.87O ATOM 1156 N ALA B2034 13.501 1.355 42.896 1.00 17.54 N ATOM 1157 CAALA B2034 12.886 2.367 43.757 1.00 18.74 C ATOM 1158 CB ALA B2034 13.5652.369 45.123 1.00 18.99 C ATOM 1159 C ALA B2034 12.925 3.771 43.145 1.0018.65 C ATOM 1160 O ALA B2034 11.930 4.503 43.188 1.00 18.77 O ATOM 1161N LEU B2035 14.066 4.148 42.572 1.00 18.26 N ATOM 1162 CA LEU B203514.216 5.470 41.962 1.00 19.09 C ATOM 1163 CB LEU B2035 15.697 5.74241.665 1.00 20.60 C ATOM 1164 CG LEU B2035 16.154 7.182 41.435 1.0022.12 C ATOM 1165 CD1 LEU B2035 15.976 8.015 42.714 1.00 23.52 C ATOM1166 CD2 LEU B2035 17.618 7.173 41.031 1.00 24.30 C ATOM 1167 C LEUB2035 13.383 5.610 40.680 1.00 18.93 C ATOM 1168 O LEU B2035 12.8016.670 40.430 1.00 19.57 O ATOM 1169 N GLU B2036 13.333 4.559 39.858 1.0018.62 N ATOM 1170 CA GLU B2036 12.533 4.604 38.626 1.00 18.35 C ATOM1171 CB GLU B2036 12.733 3.327 37.784 1.00 17.51 C ATOM 1172 CG GLUB2036 14.085 3.215 37.042 1.00 15.99 C ATOM 1173 CD GLU B2036 14.3001.848 36.391 1.00 16.12 C ATOM 1174 OE1 GLU B2036 15.007 1.777 35.3611.00 15.21 O ATOM 1175 OE2 GLU B2036 13.781 0.836 36.911 1.00 15.16 OATOM 1176 C GLU B2036 11.039 4.744 38.982 1.00 19.23 C ATOM 1177 O GLUB2036 10.290 5.440 38.296 1.00 19.60 O ATOM 1178 N MET B2037 10.6164.074 40.051 1.00 19.86 N ATOM 1179 CA MET B2037 9.219 4.123 40.501 1.0021.88 C ATOM 1180 CB MET B2037 9.008 3.086 41.615 1.00 22.85 C ATOM 1181CG MET B2037 7.623 3.055 42.236 1.00 25.86 C ATOM 1182 SD MET B20376.356 2.391 41.143 1.00 28.53 S ATOM 1183 CE MET B2037 6.759 0.62641.201 1.00 27.97 C ATOM 1184 C MET B2037 8.834 5.528 41.000 1.00 22.03C ATOM 1185 O MET B2037 7.716 6.006 40.772 1.00 22.35 O ATOM 1186 N GLUB2038 9.759 6.187 41.687 1.00 22.54 N ATOM 1187 CA GLU B2038 9.501 7.52842.194 1.00 23.34 C ATOM 1188 CB GLU B2038 10.663 7.973 43.101 1.0023.49 C ATOM 1189 CG GLU B2038 10.475 7.496 44.550 1.00 24.52 C ATOM1190 CD GLU B2038 11.772 7.284 45.326 1.00 25.50 C ATOM 1191 OE1 GLUB2038 12.785 7.962 45.036 1.00 25.67 O ATOM 1192 OE2 GLU B2038 11.7656.439 46.251 1.00 25.94 O ATOM 1193 C GLU B2038 9.252 8.513 41.046 1.0023.18 C ATOM 1194 O GLU B2038 8.512 9.482 41.200 1.00 23.42 O ATOM 1195N ARG B2039 9.854 8.250 39.888 1.00 23.18 N ATOM 1196 CA ARG B2039 9.6599.097 38.713 1.00 23.42 C ATOM 1197 CB ARG B2039 10.801 8.888 37.7101.00 24.21 C ATOM 1198 CG ARG B2039 10.566 9.517 36.338 1.00 24.82 CATOM 1199 CD ARG B2039 10.414 11.027 36.415 0.05 24.52 C ATOM 1200 NEARG B2039 10.169 11.609 35.099 0.05 24.58 N ATOM 1201 CZ ARG B2039 9.99512.908 34.873 0.05 24.54 C ATOM 1202 NH1 ARG B2039 9.776 13.344 33.6400.05 24.55 N ATOM 1203 NH2 ARG B2039 10.039 13.771 35.879 0.05 24.55 NATOM 1204 C ARG B2039 8.323 8.738 38.057 1.00 22.97 C ATOM 1205 O ARGB2039 7.591 9.614 37.594 1.00 23.62 O ATOM 1206 N PHE B2040 8.015 7.44338.037 1.00 22.59 N ATOM 1207 CA PHE B2040 6.777 6.914 37.456 1.00 23.04C ATOM 1208 CB PHE B2040 6.769 5.381 37.598 1.00 23.27 C ATOM 1209 CGPHE B2040 5.520 4.705 37.082 1.00 24.49 C ATOM 1210 CD1 PHE B2040 5.2704.604 35.716 1.00 24.75 C ATOM 1211 CD2 PHE B2040 4.611 4.125 37.9711.00 24.92 C ATOM 1212 CE1 PHE B2040 4.135 3.930 35.240 1.00 25.22 CATOM 1213 CE2 PHE B2040 3.473 3.451 37.509 1.00 24.72 C ATOM 1214 CZ PHEB2040 3.236 3.353 36.139 1.00 25.48 C ATOM 1215 C PHE B2040 5.529 7.50638.126 1.00 23.15 C ATOM 1216 O PHE B2040 4.558 7.841 37.448 1.00 22.73O ATOM 1217 N THR B2041 5.559 7.636 39.452 1.00 23.63 N ATOM 1218 CA THRB2041 4.407 8.165 40.186 1.00 25.06 C ATOM 1219 CB THR B2041 4.487 7.81941.701 1.00 24.62 C ATOM 1220 OG1 THR B2041 5.710 8.322 42.250 1.0024.25 O ATOM 1221 CG2 THR B2041 4.421 6.311 41.910 1.00 24.17 C ATOM1222 C THR B2041 4.156 9.669 40.050 1.00 25.84 C ATOM 1223 O THR B20413.089 10.155 40.442 1.00 26.22 O ATOM 1224 N SER B2042 5.119 10.41239.508 1.00 27.24 N ATOM 1225 CA SER B2042 4.939 11.856 39.346 1.0028.70 C ATOM 1226 CB SER B2042 6.256 12.605 39.605 1.00 29.90 C ATOM1227 OG SER B2042 7.260 12.270 38.658 1.00 31.49 O ATOM 1228 C SER B20424.404 12.214 37.959 1.00 29.44 C ATOM 1229 O SER B2042 4.245 13.39237.632 1.00 28.96 O ATOM 1230 N LEU B2043 4.127 11.192 37.151 1.00 29.93N ATOM 1231 CA LEU B2043 3.598 11.379 35.797 1.00 30.98 C ATOM 1232 CBLEU B2043 4.466 10.622 34.779 1.00 30.83 C ATOM 1233 CG LEU B2043 5.92511.061 34.614 1.00 30.66 C ATOM 1234 CD1 LEU B2043 6.690 10.037 33.7781.00 31.31 C ATOM 1235 CD2 LEU B2043 5.970 12.431 33.960 1.00 31.38 CATOM 1236 C LEU B2043 2.160 10.864 35.712 1.00 31.75 C ATOM 1237 O LEUB2043 1.711 10.106 36.573 1.00 31.45 O ATOM 1238 N LYS B2044 1.44011.264 34.668 1.00 33.21 N ATOM 1239 CA LYS B2044 0.059 10.820 34.4971.00 34.53 C ATOM 1240 CB LYS B2044 −0.904 11.853 35.100 1.00 35.00 CATOM 1241 CG LYS B2044 −2.362 11.415 35.118 0.05 34.86 C ATOM 1242 CDLYS B2044 −3.267 12.481 35.714 0.05 34.96 C ATOM 1243 CE LYS B2044−4.718 12.025 35.718 0.05 34.95 C ATOM 1244 NZ LYS B2044 −5.625 13.05636.293 0.05 35.07 N ATOM 1245 C LYS B2044 −0.311 10.580 33.035 1.0035.45 C ATOM 1246 O LYS B2044 0.422 10.960 32.121 1.00 35.43 O ATOM 1247N GLY B2045 −1.454 9.934 32.829 1.00 36.33 N ATOM 1248 CA GLY B2045−1.940 9.671 31.488 1.00 37.45 C ATOM 1249 C GLY B2045 −1.031 8.86930.579 1.00 38.02 C ATOM 1250 O GLY B2045 −0.215 8.065 31.036 1.00 38.35O ATOM 1251 N ARG B2046 −1.187 9.099 29.279 1.00 38.11 N ATOM 1252 CAARG B2046 −0.414 8.409 28.250 1.00 38.00 C ATOM 1253 CB ARG B2046 −0.7189.026 26.882 1.00 38.22 C ATOM 1254 CG ARG B2046 −2.203 9.241 26.6350.05 38.32 C ATOM 1255 CD ARG B2046 −2.469 9.951 25.319 0.05 38.47 CATOM 1256 NE ARG B2046 −2.193 9.103 24.164 0.05 38.58 N ATOM 1257 CZ ARGB2046 −2.418 9.462 22.904 0.05 38.64 C ATOM 1258 NH1 ARG B2046 −2.1388.626 21.915 0.05 38.67 N ATOM 1259 NH2 ARG B2046 −2.925 10.657 22.6330.05 38.67 N ATOM 1260 C ARG B2046 1.083 8.472 28.516 1.00 37.79 C ATOM1261 O ARG B2046 1.809 7.514 28.262 1.00 37.64 O ATOM 1262 N ARG B20471.534 9.611 29.031 1.00 37.35 N ATOM 1263 CA ARG B2047 2.945 9.82729.327 1.00 36.86 C ATOM 1264 CB ARG B2047 3.139 11.262 29.824 1.0038.35 C ATOM 1265 CG ARG B2047 4.529 11.834 29.622 1.00 40.01 C ATOM1266 CD ARG B2047 4.591 13.258 30.156 1.00 41.52 C ATOM 1267 NE ARGB2047 5.880 13.894 29.903 1.00 43.12 N ATOM 1268 CZ ARG B2047 6.27615.030 30.471 1.00 44.06 C ATOM 1269 NH1 ARG B2047 7.467 15.539 30.1801.00 44.67 N ATOM 1270 NH2 ARG B2047 5.486 15.654 31.336 1.00 44.50 NATOM 1271 C ARG B2047 3.460 8.826 30.368 1.00 35.56 C ATOM 1272 O ARGB2047 4.631 8.454 30.354 1.00 34.93 O ATOM 1273 N GLN B2048 2.578 8.38831.263 1.00 34.21 N ATOM 1274 CA GLN B2048 2.947 7.433 32.305 1.00 32.54C ATOM 1275 CB GLN B2048 1.866 7.413 33.396 1.00 33.03 C ATOM 1276 CGGLN B2048 2.203 6.564 34.616 1.00 32.53 C ATOM 1277 CD GLN B2048 1.2036.741 35.751 1.00 33.31 C ATOM 1278 OE1 GLN B2048 0.009 6.499 35.5861.00 32.97 O ATOM 1279 NE2 GLN B2048 1.694 7.164 36.914 1.00 33.17 NATOM 1280 C GLN B2048 3.161 6.021 31.740 1.00 31.47 C ATOM 1281 O GLNB2048 4.119 5.340 32.106 1.00 31.22 O ATOM 1282 N ILE B2049 2.269 5.58930.852 1.00 29.87 N ATOM 1283 CA ILE B2049 2.366 4.266 30.233 1.00 28.47C ATOM 1284 CB ILE B2049 1.087 3.936 29.417 1.00 28.92 C ATOM 1285 CG2ILE B2049 1.263 2.627 28.667 1.00 29.21 C ATOM 1286 CG1 ILE B2049 −0.1303.858 30.346 1.00 29.32 C ATOM 1287 CD1 ILE B2049 −0.118 2.675 31.3051.00 28.99 C ATOM 1288 C ILE B2049 3.577 4.191 29.292 1.00 27.84 C ATOM1289 O ILE B2049 4.172 3.127 29.116 1.00 27.30 O ATOM 1290 N GLU B20503.933 5.321 28.688 1.00 26.72 N ATOM 1291 CA GLU B2050 5.073 5.37327.774 1.00 26.84 C ATOM 1292 CB GLU B2050 5.060 6.692 26.985 1.00 27.77C ATOM 1293 CG GLU B2050 6.298 6.973 26.119 1.00 30.05 C ATOM 1294 CDGLU B2050 6.456 6.027 24.927 1.00 31.34 C ATOM 1295 OE1 GLU B2050 5.4435.718 24.262 1.00 32.49 O ATOM 1296 OE2 GLU B2050 7.603 5.610 24.6431.00 31.18 O ATOM 1297 C GLU B2050 6.397 5.223 28.520 1.00 25.29 C ATOM1298 O GLU B2050 7.339 4.621 27.994 1.00 24.70 O ATOM 1299 N TYR B20516.471 5.767 29.737 1.00 23.32 N ATOM 1300 CA TYR B2051 7.696 5.67530.537 1.00 21.39 C ATOM 1301 CB TYR B2051 7.576 6.526 31.821 1.00 21.45C ATOM 1302 CG TYR B2051 8.819 6.522 32.712 1.00 20.60 C ATOM 1303 CD1TYR B2051 8.974 5.577 33.728 1.00 20.47 C ATOM 1304 CE1 TYR B2051 10.1285.547 34.526 1.00 20.26 C ATOM 1305 CD2 TYR B2051 9.852 7.444 32.5121.00 20.44 C ATOM 1306 CE2 TYR B2051 11.012 7.420 33.302 1.00 20.69 CATOM 1307 CZ TYR B2051 11.141 6.469 34.306 1.00 20.69 C ATOM 1308 OH TYRB2051 12.277 6.449 35.094 1.00 21.32 O ATOM 1309 C TYR B2051 7.978 4.21230.885 1.00 20.75 C ATOM 1310 O TYR B2051 9.085 3.718 30.658 1.00 19.49O ATOM 1311 N LEU B2052 6.968 3.520 31.413 1.00 19.18 N ATOM 1312 CA LEUB2052 7.096 2.109 31.788 1.00 18.14 C ATOM 1313 CB LEU B2052 5.782 1.61632.419 1.00 18.69 C ATOM 1314 CG LEU B2052 5.668 0.154 32.868 1.00 19.58C ATOM 1315 CD1 LEU B2052 6.783 −0.189 33.861 1.00 19.24 C ATOM 1316 CD2LEU B2052 4.299 −0.070 33.511 1.00 20.41 C ATOM 1317 C LEU B2052 7.4761.209 30.598 1.00 17.54 C ATOM 1318 O LEU B2052 8.347 0.347 30.719 1.0016.53 O ATOM 1319 N ALA B2053 6.828 1.411 29.453 1.00 16.29 N ATOM 1320CA ALA B2053 7.115 0.600 28.262 1.00 16.39 C ATOM 1321 CB ALA B20536.106 0.926 27.154 1.00 16.13 C ATOM 1322 C ALA B2053 8.550 0.794 27.7441.00 15.79 C ATOM 1323 O ALA B2053 9.206 −0.169 27.325 1.00 16.28 O ATOM1324 N GLY B2054 9.034 2.033 27.771 1.00 15.48 N ATOM 1325 CA GLY B205410.391 2.311 27.316 1.00 15.32 C ATOM 1326 C GLY B2054 11.471 1.70128.201 1.00 16.07 C ATOM 1327 O GLY B2054 12.550 1.309 27.716 1.00 14.96O ATOM 1328 N ARG B2055 11.208 1.633 29.506 1.00 15.22 N ATOM 1329 CAARG B2055 12.179 1.040 30.430 1.00 16.35 C ATOM 1330 CB ARG B2055 11.7901.353 31.886 1.00 17.42 C ATOM 1331 CG ARG B2055 12.545 2.543 32.5141.00 19.58 C ATOM 1332 CD ARG B2055 12.545 3.794 31.623 1.00 21.46 CATOM 1333 NE ARG B2055 13.423 4.838 32.153 1.00 21.36 N ATOM 1334 CZ ARGB2055 13.695 5.986 31.534 1.00 22.03 C ATOM 1335 NH1 ARG B2055 13.1556.256 30.353 1.00 22.33 N ATOM 1336 NH2 ARG B2055 14.520 6.865 32.0941.00 21.30 N ATOM 1337 C ARG B2055 12.261 −0.479 30.194 1.00 16.15 CATOM 1338 O ARG B2055 13.339 −1.079 30.277 1.00 15.13 O ATOM 1339 N TRPB2056 11.119 −1.090 29.884 1.00 16.30 N ATOM 1340 CA TRP B2056 11.055−2.528 29.608 1.00 17.26 C ATOM 1341 CB TRP B2056 9.592 −2.966 29.4251.00 19.31 C ATOM 1342 CG TRP B2056 9.393 −4.449 29.444 1.00 22.46 CATOM 1343 CD2 TRP B2056 9.458 −5.335 28.325 1.00 24.24 C ATOM 1344 CE2TRP B2056 9.234 −6.644 28.813 1.00 25.47 C ATOM 1345 CE3 TRP B2056 9.684−5.153 26.954 1.00 25.79 C ATOM 1346 CD1 TRP B2056 9.139 −5.234 30.5401.00 23.87 C ATOM 1347 NE1 TRP B2056 9.041 −6.552 30.167 1.00 24.64 NATOM 1348 CZ2 TRP B2056 9.231 −7.763 27.979 1.00 26.38 C ATOM 1349 CZ3TRP B2056 9.681 −6.270 26.122 1.00 27.06 C ATOM 1350 CH2 TRP B2056 9.455−7.559 26.641 1.00 27.05 C ATOM 1351 C TRP B2056 11.843 −2.850 28.3271.00 16.16 C ATOM 1352 O TRP B2056 12.642 −3.794 28.288 1.00 16.26 OATOM 1353 N SER B2057 11.608 −2.053 27.288 1.00 15.01 N ATOM 1354 CA SERB2057 12.265 −2.208 25.980 1.00 14.82 C ATOM 1355 CB SER B2057 11.678−1.155 25.017 1.00 15.72 C ATOM 1356 OG SER B2057 12.069 −1.352 23.6701.00 19.47 O ATOM 1357 C SER B2057 13.807 −2.052 26.087 1.00 14.21 CATOM 1358 O SER B2057 14.581 −2.816 25.471 1.00 12.39 O ATOM 1359 N ALAB2058 14.246 −1.072 26.873 1.00 12.21 N ATOM 1360 CA ALA B2058 15.680−0.810 27.052 1.00 12.92 C ATOM 1361 CB ALA B2058 15.878 0.516 27.8001.00 12.17 C ATOM 1362 C ALA B2058 16.398 −1.949 27.801 1.00 12.59 CATOM 1363 O ALA B2058 17.507 −2.354 27.428 1.00 11.75 O ATOM 1364 N LYSB2059 15.772 −2.455 28.861 1.00 12.47 N ATOM 1365 CA LYS B2059 16.368−3.546 29.634 1.00 13.35 C ATOM 1366 CB LYS B2059 15.579 −3.757 30.9471.00 14.19 C ATOM 1367 CG LYS B2059 15.656 −2.538 31.896 1.00 14.71 CATOM 1368 CD LYS B2059 14.961 −2.754 33.258 1.00 15.04 C ATOM 1369 CELYS B2059 15.045 −1.488 34.124 1.00 16.38 C ATOM 1370 NZ LYS B205914.590 −1.651 35.545 1.00 15.99 N ATOM 1371 C LYS B2059 16.459 −4.84628.814 1.00 14.13 C ATOM 1372 O LYS B2059 17.406 −5.632 28.992 1.0013.94 O ATOM 1373 N GLU B2060 15.500 −5.072 27.907 1.00 13.55 N ATOM1374 CA GLU B2060 15.535 −6.276 27.066 1.00 14.73 C ATOM 1375 CB GLUB2060 14.160 −6.552 26.436 1.00 16.24 C ATOM 1376 CG GLU B2060 14.173−7.696 25.413 1.00 20.48 C ATOM 1377 CD GLU B2060 14.283 −9.089 26.0371.00 23.43 C ATOM 1378 OE1 GLU B2060 14.802 −9.230 27.168 1.00 26.30 OATOM 1379 OE2 GLU B2060 13.860 −10.061 25.376 1.00 25.45 O ATOM 1380 CGLU B2060 16.608 −6.174 25.960 1.00 13.95 C ATOM 1381 O GLU B2060 17.238−7.178 25.609 1.00 13.52 O ATOM 1382 N ALA B2061 16.819 −4.971 25.4181.00 13.22 N ATOM 1383 CA ALA B2061 17.838 −4.765 24.379 1.00 13.62 CATOM 1384 CB ALA B2061 17.740 −3.332 23.801 1.00 13.16 C ATOM 1385 C ALAB2061 19.241 −5.022 24.950 1.00 13.67 C ATOM 1386 O ALA B2061 20.107−5.576 24.257 1.00 14.02 O ATOM 1387 N PHE B2062 19.463 −4.630 26.2071.00 13.22 N ATOM 1388 CA PHE B2062 20.760 −4.860 26.873 1.00 14.50 CATOM 1389 CB PHE B2062 20.844 −4.049 28.185 1.00 14.44 C ATOM 1390 CGPHE B2062 22.074 −4.353 29.029 1.00 14.90 C ATOM 1391 CD1 PHE B206222.084 −5.445 29.908 1.00 15.30 C ATOM 1392 CD2 PHE B2062 23.223 −3.57128.923 1.00 15.56 C ATOM 1393 CE1 PHE B2062 23.223 −5.752 30.663 1.0015.94 C ATOM 1394 CE2 PHE B2062 24.375 −3.869 29.678 1.00 15.34 C ATOM1395 CZ PHE B2062 24.370 −4.961 30.545 1.00 15.50 C ATOM 1396 C PHEB2062 20.969 −6.363 27.147 1.00 14.72 C ATOM 1397 O PHE B2062 22.063−6.894 26.938 1.00 14.93 O ATOM 1398 N SER B2063 19.922 −7.052 27.5991.00 14.63 N ATOM 1399 CA SER B2063 20.016 −8.490 27.864 1.00 15.27 CATOM 1400 CB SER B2063 18.688 −9.021 28.415 1.00 16.20 C ATOM 1401 OGSER B2063 18.406 −8.473 29.694 1.00 18.16 O ATOM 1402 C SER B2063 20.379−9.257 26.579 1.00 15.62 C ATOM 1403 O SER B2063 21.187 −10.185 26.6071.00 14.45 O ATOM 1404 N LYS B2064 19.767 −8.872 25.459 1.00 15.61 NATOM 1405 CA LYS B2064 20.049 −9.514 24.175 1.00 16.52 C ATOM 1406 CBLYS B2064 19.012 −9.077 23.125 1.00 16.00 C ATOM 1407 CG LYS B206417.614 −9.664 23.369 1.00 15.31 C ATOM 1408 CD LYS B2064 16.563 −9.14922.365 1.00 17.09 C ATOM 1409 CE LYS B2064 16.849 −9.635 20.935 1.0018.35 C ATOM 1410 NZ LYS B2064 15.798 −9.213 19.951 1.00 19.10 N ATOM1411 C LYS B2064 21.470 −9.195 23.694 1.00 17.20 C ATOM 1412 O LYS B206422.113 −10.024 23.043 1.00 17.94 O ATOM 1413 N ALA B2065 21.962 −7.99924.014 1.00 18.06 N ATOM 1414 CA ALA B2065 23.316 −7.605 23.623 1.0019.56 C ATOM 1415 CB ALA B2065 23.545 −6.119 23.922 1.00 20.35 C ATOM1416 C ALA B2065 24.361 −8.453 24.358 1.00 21.22 C ATOM 1417 O ALA B206525.473 −8.657 23.859 1.00 20.91 O ATOM 1418 N MET B2066 24.007 −8.94025.545 1.00 22.79 N ATOM 1419 CA MET B2066 24.924 −9.774 26.331 1.0025.40 C ATOM 1420 CB MET B2066 24.690 −9.573 27.836 1.00 25.98 C ATOM1421 CG MET B2066 25.035 −8.178 28.353 1.00 28.04 C ATOM 1422 SD METB2066 26.596 −8.065 29.288 1.00 31.65 S ATOM 1423 CE MET B2066 26.043−8.670 30.858 1.00 29.68 C ATOM 1424 C MET B2066 24.761 −11.256 25.9831.00 26.28 C ATOM 1425 O MET B2066 25.539 −12.095 26.441 1.00 27.12 OATOM 1426 N GLY B2067 23.743 −11.570 25.184 1.00 26.98 N ATOM 1427 CAGLY B2067 23.501 −12.943 24.772 1.00 28.85 C ATOM 1428 C GLY B206722.447 −13.728 25.544 1.00 30.30 C ATOM 1429 O GLY B2067 22.379 −14.95025.408 1.00 30.22 O ATOM 1430 N THR B2068 21.618 −13.048 26.335 1.0031.36 N ATOM 1431 CA THR B2068 20.583 −13.729 27.120 1.00 33.00 C ATOM1432 CB THR B2068 21.043 −13.892 28.595 1.00 32.89 C ATOM 1433 OG1 THRB2068 20.057 −14.628 29.332 1.00 33.56 O ATOM 1434 CG2 THR B2068 21.253−12.528 29.248 1.00 32.58 C ATOM 1435 C THR B2068 19.217 −13.023 27.0831.00 33.93 C ATOM 1436 O THR B2068 18.867 −12.381 26.091 1.00 34.69 OATOM 1437 N GLY B2069 18.446 −13.157 28.161 1.00 35.37 N ATOM 1438 CAGLY B2069 17.132 −12.534 28.239 1.00 36.59 C ATOM 1439 C GLY B206916.890 −11.870 29.586 1.00 37.70 C ATOM 1440 O GLY B2069 17.525 −12.22130.580 1.00 38.22 O ATOM 1441 N ILE B2070 15.960 −10.918 29.631 1.0038.74 N ATOM 1442 CA ILE B2070 15.668 −10.195 30.869 1.00 39.48 C ATOM1443 CB ILE B2070 14.789 −8.948 30.595 1.00 39.69 C ATOM 1444 CG2 ILEB2070 13.430 −9.375 30.057 1.00 40.00 C ATOM 1445 CG1 ILE B2070 14.621−8.132 31.880 1.00 39.65 C ATOM 1446 CD1 ILE B2070 15.923 −7.652 32.4911.00 39.07 C ATOM 1447 C ILE B2070 15.008 −11.043 31.960 1.00 40.17 CATOM 1448 O ILE B2070 15.155 −10.748 33.150 1.00 40.22 O ATOM 1449 N SERB2071 14.283 −12.087 31.564 1.00 40.66 N ATOM 1450 CA SER B2071 13.632−12.963 32.539 1.00 41.23 C ATOM 1451 CB SER B2071 12.702 −13.965 31.8411.00 41.77 C ATOM 1452 OG SER B2071 11.623 −13.319 31.185 1.00 43.00 OATOM 1453 C SER B2071 14.694 −13.729 33.324 1.00 41.05 C ATOM 1454 O SERB2071 14.446 −14.202 34.435 1.00 41.50 O ATOM 1455 N LYS B2072 15.883−13.838 32.740 1.00 40.66 N ATOM 1456 CA LYS B2072 16.992 −14.554 33.3601.00 39.81 C ATOM 1457 CB LYS B2072 17.754 −15.336 32.286 1.00 40.65 CATOM 1458 CG LYS B2072 16.868 −16.186 31.383 1.00 41.38 C ATOM 1459 CDLYS B2072 17.686 −16.871 30.301 1.00 42.22 C ATOM 1460 CE LYS B207216.818 −17.749 29.419 1.00 42.85 C ATOM 1461 NZ LYS B2072 15.748 −16.96428.747 1.00 43.40 N ATOM 1462 C LYS B2072 17.954 −13.620 34.093 1.0038.99 C ATOM 1463 O LYS B2072 18.445 −13.947 35.174 1.00 38.73 O ATOM1464 N LEU B2073 18.214 −12.457 33.502 1.00 38.00 N ATOM 1465 CA LEUB2073 19.136 −11.480 34.082 1.00 37.21 C ATOM 1466 CB LEU B2073 19.514−10.444 33.015 1.00 37.84 C ATOM 1467 CG LEU B2073 20.842 −9.689 33.1441.00 38.45 C ATOM 1468 CD1 LEU B2073 21.202 −9.069 31.801 1.00 38.77 CATOM 1469 CD2 LEU B2073 20.738 −8.625 34.226 1.00 38.87 C ATOM 1470 CLEU B2073 18.583 −10.784 35.338 1.00 36.22 C ATOM 1471 O LEU B207319.335 −10.491 36.268 1.00 36.38 O ATOM 1472 N GLY B2074 17.276 −10.52735.366 1.00 34.86 N ATOM 1473 CA GLY B2074 16.670 −9.874 36.520 1.0032.86 C ATOM 1474 C GLY B2074 16.457 −8.376 36.351 1.00 31.51 C ATOM1475 O GLY B2074 17.415 −7.625 36.168 1.00 31.09 O ATOM 1476 N PHE B207515.204 −7.934 36.435 1.00 29.86 N ATOM 1477 CA PHE B2075 14.873 −6.51636.274 1.00 28.90 C ATOM 1478 CB PHE B2075 13.348 −6.309 36.264 1.0029.85 C ATOM 1479 CG PHE B2075 12.656 −6.885 35.062 1.00 30.57 C ATOM1480 CD1 PHE B2075 12.145 −8.177 35.090 1.00 31.57 C ATOM 1481 CD2 PHEB2075 12.502 −6.130 33.905 1.00 31.69 C ATOM 1482 CE1 PHE B2075 11.487−8.714 33.980 1.00 31.82 C ATOM 1483 CE2 PHE B2075 11.845 −6.656 32.7861.00 32.40 C ATOM 1484 CZ PHE B2075 11.336 −7.954 32.828 1.00 32.18 CATOM 1485 C PHE B2075 15.470 −5.558 37.310 1.00 27.58 C ATOM 1486 O PHEB2075 15.773 −4.409 36.983 1.00 26.85 O ATOM 1487 N GLN B2076 15.626−6.013 38.551 1.00 26.42 N ATOM 1488 CA GLN B2076 16.161 −5.156 39.6121.00 26.02 C ATOM 1489 CB GLN B2076 15.829 −5.745 40.995 1.00 26.15 CATOM 1490 CG GLN B2076 14.332 −5.838 41.292 1.00 25.92 C ATOM 1491 CDGLN B2076 13.641 −4.482 41.284 1.00 26.13 C ATOM 1492 OE1 GLN B207612.615 −4.300 40.624 1.00 25.80 O ATOM 1493 NE2 GLN B2076 14.193 −3.52842.031 1.00 25.89 N ATOM 1494 C GLN B2076 17.663 −4.892 39.524 1.0025.52 C ATOM 1495 O GLN B2076 18.195 −4.068 40.276 1.00 25.38 O ATOM1496 N ASP B2077 18.343 −5.576 38.608 1.00 25.07 N ATOM 1497 CA ASPB2077 19.789 −5.407 38.448 1.00 25.24 C ATOM 1498 CB ASP B2077 20.447−6.739 38.060 1.00 28.16 C ATOM 1499 CG ASP B2077 20.008 −7.895 38.9451.00 31.24 C ATOM 1500 OD1 ASP B2077 19.868 −7.699 40.172 1.00 32.43 OATOM 1501 OD2 ASP B2077 19.815 −9.009 38.407 1.00 34.01 O ATOM 1502 CASP B2077 20.164 −4.350 37.402 1.00 23.27 C ATOM 1503 O ASP B2077 21.347−4.096 37.173 1.00 23.32 O ATOM 1504 N LEU B2078 19.160 −3.742 36.7741.00 21.03 N ATOM 1505 CA LEU B2078 19.376 −2.717 35.746 1.00 18.79 CATOM 1506 CB LEU B2078 18.923 −3.240 34.370 1.00 18.82 C ATOM 1507 CGLEU B2078 19.560 −4.543 33.861 1.00 19.30 C ATOM 1508 CD1 LEU B207818.877 −5.001 32.575 1.00 19.23 C ATOM 1509 CD2 LEU B2078 21.040 −4.32533.622 1.00 19.43 C ATOM 1510 C LEU B2078 18.582 −1.451 36.081 1.0018.03 C ATOM 1511 O LEU B2078 17.463 −1.543 36.591 1.00 17.56 O ATOM1512 N GLU B2079 19.150 −0.276 35.792 1.00 16.76 N ATOM 1513 CA GLUB2079 18.466 0.998 36.060 1.00 15.78 C ATOM 1514 CB GLU B2079 18.9121.563 37.417 1.00 16.39 C ATOM 1515 CG GLU B2079 18.136 2.809 37.8631.00 18.61 C ATOM 1516 CD GLU B2079 18.567 3.319 39.237 1.00 19.54 CATOM 1517 OE1 GLU B2079 19.725 3.776 39.376 1.00 18.25 O ATOM 1518 OE2GLU B2079 17.743 3.257 40.180 1.00 20.67 O ATOM 1519 C GLU B2079 18.7292.029 34.944 1.00 15.93 C ATOM 1520 O GLU B2079 19.884 2.233 34.543 1.0015.32 O ATOM 1521 N VAL B2080 17.659 2.666 34.452 1.00 15.15 N ATOM 1522CA VAL B2080 17.735 3.664 33.371 1.00 15.13 C ATOM 1523 CB VAL B208016.973 3.169 32.083 1.00 14.90 C ATOM 1524 CG1 VAL B2080 17.063 4.22830.963 1.00 12.93 C ATOM 1525 CG2 VAL B2080 17.555 1.844 31.593 1.0014.67 C ATOM 1526 C VAL B2080 17.120 5.015 33.779 1.00 16.52 C ATOM 1527O VAL B2080 15.913 5.096 34.046 1.00 16.43 O ATOM 1528 N LEU B208117.941 6.069 33.815 1.00 17.23 N ATOM 1529 CA LEU B2081 17.469 7.41434.178 1.00 18.35 C ATOM 1530 CB LEU B2081 18.248 7.944 35.398 1.0018.31 C ATOM 1531 CG LEU B2081 18.457 7.034 36.621 1.00 18.74 C ATOM1532 CD1 LEU B2081 19.403 7.722 37.602 1.00 19.49 C ATOM 1533 CD2 LEUB2081 17.128 6.720 37.296 1.00 19.00 C ATOM 1534 C LEU B2081 17.6578.391 33.006 1.00 19.38 C ATOM 1535 O LEU B2081 18.257 8.040 31.984 1.0018.07 O ATOM 1536 N ASN B2082 17.148 9.616 33.159 1.00 21.21 N ATOM 1537CA ASN B2082 17.276 10.659 32.125 1.00 23.15 C ATOM 1538 CB ASN B208215.898 11.236 31.770 1.00 24.29 C ATOM 1539 CG ASN B2082 15.110 10.35130.816 1.00 25.10 C ATOM 1540 OD1 ASN B2082 15.401 10.292 29.619 1.0026.00 O ATOM 1541 ND2 ASN B2082 14.109 9.657 31.343 1.00 24.28 N ATOM1542 C ASN B2082 18.171 11.785 32.654 1.00 23.63 C ATOM 1543 O ASN B208217.988 12.228 33.785 1.00 24.09 O ATOM 1544 N ASN B2083 19.137 12.26031.864 1.00 24.20 N ATOM 1545 CA ASN B2083 20.001 13.328 32.376 1.0025.17 C ATOM 1546 CB ASN B2083 21.395 13.280 31.711 1.00 25.74 C ATOM1547 CG ASN B2083 21.405 13.770 30.270 1.00 25.64 C ATOM 1548 OD1 ASNB2083 22.425 13.652 29.584 1.00 27.52 O ATOM 1549 ND2 ASN B2083 20.29914.327 29.810 1.00 24.85 N ATOM 1550 C ASN B2083 19.356 14.718 32.2791.00 25.54 C ATOM 1551 O ASN B2083 18.214 14.844 31.831 1.00 25.60 OATOM 1552 N GLU B2084 20.067 15.759 32.706 1.00 26.28 N ATOM 1553 CA GLUB2084 19.490 17.105 32.688 1.00 27.23 C ATOM 1554 CB GLU B2084 20.37818.083 33.479 1.00 28.30 C ATOM 1555 CG GLU B2084 21.731 18.411 32.8791.00 29.51 C ATOM 1556 CD GLU B2084 22.612 19.175 33.860 1.00 31.00 CATOM 1557 OE1 GLU B2084 22.065 19.983 34.645 1.00 31.91 O ATOM 1558 OE2GLU B2084 23.847 18.976 33.847 1.00 30.61 O ATOM 1559 C GLU B2084 19.15317.675 31.307 1.00 27.45 C ATOM 1560 O GLU B2084 18.514 18.725 31.2071.00 27.41 O ATOM 1561 N ARG B2085 19.569 16.986 30.244 1.00 27.72 NATOM 1562 CA ARG B2085 19.259 17.429 28.885 1.00 27.29 C ATOM 1563 CBARG B2085 20.490 17.355 27.976 1.00 29.07 C ATOM 1564 CG ARG B208521.545 18.411 28.244 1.00 30.86 C ATOM 1565 CD ARG B2085 22.540 18.48327.089 1.00 33.01 C ATOM 1566 NE ARG B2085 23.592 19.471 27.319 1.0034.52 N ATOM 1567 CZ ARG B2085 24.556 19.337 28.221 1.00 34.97 C ATOM1568 NH1 ARG B2085 24.608 18.252 28.982 1.00 36.01 N ATOM 1569 NH2 ARGB2085 25.469 20.285 28.363 1.00 35.52 N ATOM 1570 C ARG B2085 18.14716.563 28.294 1.00 26.76 C ATOM 1571 O ARG B2085 17.642 16.838 27.2031.00 26.29 O ATOM 1572 N GLY B2086 17.777 15.508 29.018 1.00 25.36 NATOM 1573 CA GLY B2086 16.721 14.623 28.558 1.00 24.19 C ATOM 1574 C GLYB2086 17.156 13.325 27.896 1.00 23.02 C ATOM 1575 O GLY B2086 16.30512.537 27.475 1.00 22.83 O ATOM 1576 N ALA B2087 18.462 13.083 27.7981.00 21.71 N ATOM 1577 CA ALA B2087 18.938 11.848 27.172 1.00 20.63 CATOM 1578 CB ALA B2087 20.336 12.055 26.576 1.00 21.15 C ATOM 1579 C ALAB2087 18.955 10.671 28.157 1.00 19.81 C ATOM 1580 O ALA B2087 19.36410.824 29.315 1.00 18.56 O ATOM 1581 N PRO B2088 18.505 9.479 27.7071.00 18.87 N ATOM 1582 CD PRO B2088 17.864 9.249 26.397 1.00 19.36 CATOM 1583 CA PRO B2088 18.461 8.258 28.530 1.00 17.76 C ATOM 1584 CB PROB2088 17.442 7.390 27.790 1.00 18.59 C ATOM 1585 CG PRO B2088 17.7197.724 26.358 1.00 18.87 C ATOM 1586 C PRO B2088 19.831 7.571 28.650 1.0016.87 C ATOM 1587 O PRO B2088 20.593 7.559 27.688 1.00 15.25 O ATOM 1588N TYR B2089 20.130 7.002 29.826 1.00 16.14 N ATOM 1589 CA TYR B208921.405 6.311 30.078 1.00 16.26 C ATOM 1590 CB TYR B2089 22.510 7.34430.377 1.00 17.32 C ATOM 1591 CG TYR B2089 22.461 7.951 31.774 1.0016.96 C ATOM 1592 CD1 TYR B2089 23.255 7.445 32.810 1.00 18.32 C ATOM1593 CE1 TYR B2089 23.217 8.007 34.098 1.00 18.36 C ATOM 1594 CD2 TYRB2089 21.625 9.031 32.057 1.00 17.32 C ATOM 1595 CE2 TYR B2089 21.5809.595 33.332 1.00 18.67 C ATOM 1596 CZ TYR B2089 22.379 9.079 34.3471.00 18.08 C ATOM 1597 OH TYR B2089 22.337 9.654 35.601 1.00 19.43 OATOM 1598 C TYR B2089 21.313 5.311 31.250 1.00 16.51 C ATOM 1599 O TYRB2089 20.453 5.455 32.127 1.00 16.59 O ATOM 1600 N PHE B2090 22.1914.304 31.261 1.00 16.46 N ATOM 1601 CA PHE B2090 22.207 3.292 32.3381.00 16.71 C ATOM 1602 CB PHE B2090 22.803 1.953 31.855 1.00 15.86 CATOM 1603 CG PHE B2090 21.830 1.069 31.099 1.00 16.44 C ATOM 1604 CD1PHE B2090 21.652 1.216 29.724 1.00 16.03 C ATOM 1605 CD2 PHE B209021.089 0.094 31.770 1.00 16.46 C ATOM 1606 CE1 PHE B2090 20.748 0.40729.022 1.00 16.54 C ATOM 1607 CE2 PHE B2090 20.179 −0.723 31.084 1.0016.80 C ATOM 1608 CZ PHE B2090 20.008 −0.568 29.709 1.00 16.46 C ATOM1609 C PHE B2090 23.027 3.748 33.550 1.00 17.25 C ATOM 1610 O PHE B209024.245 3.938 33.445 1.00 16.58 O ATOM 1611 N SER B2091 22.372 3.90034.700 1.00 16.92 N ATOM 1612 CA SER B2091 23.068 4.312 35.922 1.0018.02 C ATOM 1613 CB SER B2091 22.148 5.177 36.802 1.00 18.33 C ATOM1614 OG SER B2091 20.902 4.535 37.052 1.00 17.93 O ATOM 1615 C SER B209123.592 3.105 36.729 1.00 18.66 C ATOM 1616 O SER B2091 24.479 3.25537.582 1.00 18.83 O ATOM 1617 N GLN B2092 23.048 1.920 36.448 1.00 18.75N ATOM 1618 CA GLN B2092 23.438 0.675 37.116 1.00 19.69 C ATOM 1619 CBGLN B2092 22.526 0.377 38.313 1.00 21.62 C ATOM 1620 CG GLN B2092 22.7261.259 39.533 1.00 25.05 C ATOM 1621 CD GLN B2092 21.981 0.730 40.7461.00 27.87 C ATOM 1622 OE1 GLN B2092 20.775 0.944 40.900 1.00 29.82 OATOM 1623 NE2 GLN B2092 22.696 0.018 41.611 1.00 29.02 N ATOM 1624 C GLNB2092 23.336 −0.512 36.151 1.00 19.36 C ATOM 1625 O GLN B2092 22.316−0.678 35.486 1.00 18.36 O ATOM 1626 N ALA B2093 24.383 −1.336 36.0941.00 18.90 N ATOM 1627 CA ALA B2093 24.411 −2.514 35.221 1.00 19.53 CATOM 1628 CB ALA B2093 24.441 −2.073 33.755 1.00 19.53 C ATOM 1629 C ALAB2093 25.625 −3.407 35.524 1.00 20.13 C ATOM 1630 O ALA B2093 26.641−2.928 36.024 1.00 20.09 O ATOM 1631 N PRO B2094 25.527 −4.720 35.2391.00 21.00 N ATOM 1632 CD PRO B2094 24.303 −5.472 34.892 1.00 21.48 CATOM 1633 CA PRO B2094 26.653 −5.631 35.498 1.00 21.95 C ATOM 1634 CBPRO B2094 25.956 −6.963 35.744 1.00 22.34 C ATOM 1635 CG PRO B209424.808 −6.905 34.739 1.00 22.42 C ATOM 1636 C PRO B2094 27.613 −5.67734.300 1.00 22.30 C ATOM 1637 O PRO B2094 27.695 −6.690 33.594 1.0022.45 O ATOM 1638 N PHE B2095 28.331 −4.572 34.083 1.00 22.56 N ATOM1639 CA PHE B2095 29.267 −4.435 32.957 1.00 23.11 C ATOM 1640 CB PHEB2095 28.471 −4.089 31.688 1.00 22.75 C ATOM 1641 CG PHE B2095 29.307−3.979 30.439 1.00 22.31 C ATOM 1642 CD1 PHE B2095 29.484 −2.746 29.8121.00 22.23 C ATOM 1643 CD2 PHE B2095 29.898 −5.107 29.876 1.00 22.30 CATOM 1644 CE1 PHE B2095 30.237 −2.639 28.640 1.00 22.73 C ATOM 1645 CE2PHE B2095 30.655 −5.012 28.705 1.00 22.36 C ATOM 1646 CZ PHE B209530.825 −3.774 28.085 1.00 21.98 C ATOM 1647 C PHE B2095 30.305 −3.34033.248 1.00 23.62 C ATOM 1648 O PHE B2095 29.965 −2.284 33.778 1.0023.96 O ATOM 1649 N SER B2096 31.561 −3.584 32.884 1.00 24.19 N ATOM1650 CA SER B2096 32.636 −2.623 33.143 1.00 25.11 C ATOM 1651 CB SERB2096 33.927 −3.376 33.477 1.00 26.30 C ATOM 1652 OG SER B2096 33.722−4.306 34.523 1.00 28.33 O ATOM 1653 C SER B2096 32.954 −1.591 32.0501.00 24.46 C ATOM 1654 O SER B2096 33.606 −0.583 32.332 1.00 25.13 OATOM 1655 N GLY B2097 32.513 −1.828 30.818 1.00 23.39 N ATOM 1656 CA GLYB2097 32.818 −0.891 29.739 1.00 21.60 C ATOM 1657 C GLY B2097 31.8230.242 29.527 1.00 20.27 C ATOM 1658 O GLY B2097 31.138 0.651 30.460 1.0020.10 O ATOM 1659 N LYS B2098 31.756 0.758 28.299 1.00 19.44 N ATOM 1660CA LYS B2098 30.822 1.836 27.954 1.00 17.90 C ATOM 1661 CB LYS B209831.472 2.822 26.978 1.00 20.19 C ATOM 1662 CG LYS B2098 32.604 3.65127.561 1.00 21.96 C ATOM 1663 CD LYS B2098 33.055 4.682 26.543 1.0024.18 C ATOM 1664 CE LYS B2098 34.115 5.612 27.103 1.00 25.70 C ATOM1665 NZ LYS B2098 34.538 6.626 26.087 1.00 27.22 N ATOM 1666 C LYS B209829.561 1.256 27.309 1.00 16.51 C ATOM 1667 O LYS B2098 29.647 0.29826.543 1.00 14.73 O ATOM 1668 N ILE B2099 28.401 1.844 27.621 1.00 15.59N ATOM 1669 CA ILE B2099 27.107 1.395 27.086 1.00 15.02 C ATOM 1670 CBILE B2099 26.144 0.954 28.236 1.00 15.10 C ATOM 1671 CG2 ILE B209924.823 0.429 27.647 1.00 16.11 C ATOM 1672 CG1 ILE B2099 26.790 −0.13829.095 1.00 15.18 C ATOM 1673 CD1 ILE B2099 25.994 −0.462 30.363 1.0016.41 C ATOM 1674 C ILE B2099 26.406 2.533 26.308 1.00 14.43 C ATOM 1675O ILE B2099 26.039 3.551 26.900 1.00 14.51 O ATOM 1676 N TRP B210026.207 2.359 25.000 1.00 13.72 N ATOM 1677 CA TRP B2100 25.547 3.38124.173 1.00 13.62 C ATOM 1678 CB TRP B2100 26.342 3.558 22.864 1.0013.58 C ATOM 1679 CG TRP B2100 27.817 3.938 23.093 1.00 13.89 C ATOM1680 CD2 TRP B2100 28.334 5.257 23.347 1.00 13.95 C ATOM 1681 CE2 TRPB2100 29.726 5.126 23.597 1.00 14.82 C ATOM 1682 CE3 TRP B2100 27.7556.535 23.395 1.00 14.46 C ATOM 1683 CD1 TRP B2100 28.890 3.085 23.1871.00 14.49 C ATOM 1684 NE1 TRP B2100 30.041 3.795 23.492 1.00 14.89 NATOM 1685 CZ2 TRP B2100 30.546 6.230 23.895 1.00 15.47 C ATOM 1686 CZ3TRP B2100 28.577 7.640 23.697 1.00 15.28 C ATOM 1687 CH2 TRP B210029.955 7.472 23.942 1.00 14.88 C ATOM 1688 C TRP B2100 24.071 2.99823.886 1.00 13.84 C ATOM 1689 O TRP B2100 23.816 1.995 23.214 1.00 13.89O ATOM 1690 N LEU B2101 23.120 3.808 24.379 1.00 13.08 N ATOM 1691 CALEU B2101 21.657 3.557 24.239 1.00 12.41 C ATOM 1692 CB LEU B2101 21.0593.267 25.634 1.00 13.29 C ATOM 1693 CG LEU B2101 19.524 3.353 25.8251.00 12.98 C ATOM 1694 CD1 LEU B2101 18.889 2.043 25.355 1.00 12.28 CATOM 1695 CD2 LEU B2101 19.156 3.601 27.303 1.00 12.42 C ATOM 1696 C LEUB2101 20.796 4.674 23.602 1.00 11.67 C ATOM 1697 O LEU B2101 21.0635.858 23.811 1.00 11.61 O ATOM 1698 N SER B2102 19.760 4.287 22.844 1.0011.90 N ATOM 1699 CA SER B2102 18.799 5.237 22.237 1.00 11.37 C ATOM1700 CB SER B2102 19.212 5.616 20.810 1.00 11.79 C ATOM 1701 OG SERB2102 18.405 6.679 20.308 1.00 9.95 O ATOM 1702 C SER B2102 17.371 4.63422.219 1.00 11.48 C ATOM 1703 O SER B2102 17.220 3.421 22.026 1.00 11.63O ATOM 1704 N ILE B2103 16.351 5.482 22.425 1.00 10.47 N ATOM 1705 CAILE B2103 14.912 5.096 22.465 1.00 10.97 C ATOM 1706 CB ILE B2103 14.3375.250 23.934 1.00 11.04 C ATOM 1707 CG2 ILE B2103 12.852 4.835 23.9811.00 11.15 C ATOM 1708 CG1 ILE B2103 15.136 4.390 24.924 1.00 10.41 CATOM 1709 CD1 ILE B2103 14.781 4.658 26.424 1.00 10.59 C ATOM 1710 C ILEB2103 14.042 5.995 21.536 1.00 11.56 C ATOM 1711 O ILE B2103 14.3277.184 21.393 1.00 11.36 O ATOM 1712 N SER B2104 12.994 5.435 20.915 1.0013.13 N ATOM 1713 CA SER B2104 12.073 6.214 20.054 1.00 14.88 C ATOM1714 CB SER B2104 12.582 6.263 18.603 1.00 15.92 C ATOM 1715 OG SERB2104 11.787 7.132 17.789 1.00 16.21 O ATOM 1716 C SER B2104 10.6525.617 20.070 1.00 15.87 C ATOM 1717 O SER B2104 10.485 4.418 20.297 1.0015.32 O ATOM 1718 N HIS B2105 9.623 6.429 19.822 1.00 17.79 N ATOM 1719CA HIS B2105 8.266 5.872 19.833 1.00 19.31 C ATOM 1720 CB HIS B21057.683 5.921 21.249 1.00 21.32 C ATOM 1721 CG HIS B2105 7.405 7.30621.746 1.00 23.02 C ATOM 1722 CD2 HIS B2105 6.279 8.058 21.704 1.0025.09 C ATOM 1723 ND1 HIS B2105 8.363 8.086 22.356 1.00 25.22 N ATOM1724 CE1 HIS B2105 7.841 9.260 22.669 1.00 25.65 C ATOM 1725 NE2 HISB2105 6.577 9.269 22.285 1.00 26.41 N ATOM 1726 C HIS B2105 7.237 6.48618.870 1.00 20.14 C ATOM 1727 O HIS B2105 7.453 7.560 18.305 1.00 18.58O ATOM 1728 N THR B2106 6.128 5.763 18.687 1.00 20.92 N ATOM 1729 CA THRB2106 5.008 6.208 17.852 1.00 23.37 C ATOM 1730 CB THR B2106 4.758 5.30216.612 1.00 23.62 C ATOM 1731 OG1 THR B2106 4.237 4.035 17.039 1.0024.37 O ATOM 1732 CG2 THR B2106 6.043 5.092 15.820 1.00 23.72 C ATOM1733 C THR B2106 3.766 6.106 18.735 1.00 23.79 C ATOM 1734 O THR B21063.867 5.875 19.937 1.00 24.63 O ATOM 1735 N ASP B2107 2.591 6.255 18.1381.00 24.86 N ATOM 1736 CA ASP B2107 1.355 6.176 18.906 1.00 24.83 C ATOM1737 CB ASP B2107 0.189 6.691 18.059 0.05 24.72 C ATOM 1738 CG ASP B2107−0.652 7.716 18.790 0.05 24.62 C ATOM 1739 OD1 ASP B2107 −1.227 7.37219.844 0.05 24.64 O ATOM 1740 OD2 ASP B2107 −0.738 8.867 18.312 0.0524.51 O ATOM 1741 C ASP B2107 1.043 4.763 19.403 1.00 24.92 C ATOM 1742O ASP B2107 0.368 4.598 20.421 1.00 26.07 O ATOM 1743 N GLN B2108 1.5353.745 18.701 1.00 24.68 N ATOM 1744 CA GLN B2108 1.255 2.361 19.086 1.0024.22 C ATOM 1745 CB GLN B2108 0.522 1.652 17.939 1.00 25.96 C ATOM 1746CG GLN B2108 −0.753 2.352 17.462 1.00 27.90 C ATOM 1747 CD GLN B2108−1.328 1.732 16.189 1.00 29.69 C ATOM 1748 OE1 GLN B2108 −2.371 1.07316.215 1.00 31.19 O ATOM 1749 NE2 GLN B2108 −0.641 1.940 15.069 1.0030.55 N ATOM 1750 C GLN B2108 2.450 1.489 19.517 1.00 23.66 C ATOM 1751O GLN B2108 2.246 0.490 20.216 1.00 22.94 O ATOM 1752 N PHE B2109 3.6721.854 19.115 1.00 22.58 N ATOM 1753 CA PHE B2109 4.869 1.058 19.450 1.0022.19 C ATOM 1754 CB PHE B2109 5.440 0.378 18.187 1.00 23.42 C ATOM 1755CG PHE B2109 4.409 −0.256 17.287 1.00 25.28 C ATOM 1756 CD1 PHE B21093.830 0.469 16.248 1.00 26.47 C ATOM 1757 CD2 PHE B2109 4.038 −1.58617.459 1.00 26.35 C ATOM 1758 CE1 PHE B2109 2.894 −0.123 15.386 1.0026.84 C ATOM 1759 CE2 PHE B2109 3.106 −2.190 16.607 1.00 27.41 C ATOM1760 CZ PHE B2109 2.534 −1.454 15.567 1.00 27.07 C ATOM 1761 C PHE B21096.031 1.852 20.088 1.00 20.94 C ATOM 1762 O PHE B2109 6.034 3.082 20.0861.00 20.73 O ATOM 1763 N VAL B2110 7.020 1.128 20.619 1.00 20.20 N ATOM1764 CA VAL B2110 8.225 1.737 21.210 1.00 18.93 C ATOM 1765 CB VAL B21108.115 1.867 22.761 1.00 19.35 C ATOM 1766 CG1 VAL B2110 7.968 0.49623.404 1.00 21.12 C ATOM 1767 CG2 VAL B2110 9.339 2.595 23.316 1.0019.95 C ATOM 1768 C VAL B2110 9.423 0.846 20.845 1.00 18.01 C ATOM 1769O VAL B2110 9.295 −0.380 20.827 1.00 17.84 O ATOM 1770 N THR B211110.576 1.450 20.548 1.00 16.67 N ATOM 1771 CA THR B2111 11.768 0.67820.170 1.00 15.96 C ATOM 1772 CB THR B2111 11.950 0.693 18.628 1.0017.10 C ATOM 1773 OG1 THR B2111 13.011 −0.201 18.258 1.00 21.79 O ATOM1774 CG2 THR B2111 12.283 2.096 18.141 1.00 17.28 C ATOM 1775 C THRB2111 13.049 1.203 20.839 1.00 14.55 C ATOM 1776 O THR B2111 13.1222.380 21.194 1.00 12.59 O ATOM 1777 N ALA B2112 14.044 0.326 21.005 1.0013.42 N ATOM 1778 CA ALA B2112 15.325 0.680 21.644 1.00 12.71 C ATOM1779 CB ALA B2112 15.247 0.379 23.145 1.00 12.85 C ATOM 1780 C ALA B211216.516 −0.078 21.024 1.00 12.80 C ATOM 1781 O ALA B2112 16.348 −1.19620.535 1.00 13.45 O ATOM 1782 N SER B2113 17.709 0.527 21.060 1.00 12.54N ATOM 1783 CA SER B2113 18.937 −0.077 20.498 1.00 12.67 C ATOM 1784 CBSER B2113 19.222 0.539 19.115 1.00 12.72 C ATOM 1785 OG SER B2113 20.4020.007 18.523 1.00 13.88 O ATOM 1786 C SER B2113 20.152 0.142 21.443 1.0011.86 C ATOM 1787 O SER B2113 20.326 1.247 21.973 1.00 12.14 O ATOM 1788N VAL B2114 20.967 −0.905 21.636 1.00 10.76 N ATOM 1789 CA VAL B211422.157 −0.885 22.526 1.00 11.02 C ATOM 1790 CB VAL B2114 21.912 −1.74823.810 1.00 10.07 C ATOM 1791 CG1 VAL B2114 23.204 −1.874 24.619 1.0012.63 C ATOM 1792 CG2 VAL B2114 20.808 −1.124 24.689 1.00 11.23 C ATOM1793 C VAL B2114 23.451 −1.438 21.880 1.00 11.08 C ATOM 1794 O VAL B211423.408 −2.477 21.204 1.00 10.49 O ATOM 1795 N ILE B2115 24.584 −0.75322.093 1.00 11.85 N ATOM 1796 CA ILE B2115 25.905 −1.198 21.585 1.0011.88 C ATOM 1797 CB ILE B2115 26.485 −0.236 20.492 1.00 12.44 C ATOM1798 CG2 ILE B2115 27.841 −0.756 19.999 1.00 12.78 C ATOM 1799 CG1 ILEB2115 25.529 −0.134 19.300 1.00 12.56 C ATOM 1800 CD1 ILE B2115 25.8890.986 18.331 1.00 12.68 C ATOM 1801 C ILE B2115 26.883 −1.197 22.7821.00 12.95 C ATOM 1802 O ILE B2115 26.966 −0.197 23.507 1.00 13.03 OATOM 1803 N LEU B2116 27.600 −2.306 22.994 1.00 12.77 N ATOM 1804 CA LEUB2116 28.559 −2.432 24.115 1.00 14.04 C ATOM 1805 CB LEU B2116 28.353−3.785 24.830 1.00 13.62 C ATOM 1806 CG LEU B2116 26.929 −4.093 25.3491.00 14.05 C ATOM 1807 CD1 LEU B2116 26.866 −5.489 25.971 1.00 15.37 CATOM 1808 CD2 LEU B2116 26.520 −3.055 26.384 1.00 14.15 C ATOM 1809 CLEU B2116 30.020 −2.296 23.630 1.00 14.81 C ATOM 1810 O LEU B2116 30.381−2.839 22.582 1.00 14.52 O ATOM 1811 N GLU B2117 30.858 −1.605 24.4091.00 16.40 N ATOM 1812 CA GLU B2117 32.255 −1.353 24.027 1.00 18.58 CATOM 1813 CB GLU B2117 32.344 0.062 23.426 1.00 18.84 C ATOM 1814 CG GLUB2117 33.737 0.570 23.061 1.00 21.74 C ATOM 1815 CD GLU B2117 33.7031.977 22.450 1.00 23.34 C ATOM 1816 OE1 GLU B2117 33.161 2.908 23.0981.00 22.55 O ATOM 1817 OE2 GLU B2117 34.221 2.153 21.322 1.00 24.09 OATOM 1818 C GLU B2117 33.247 −1.495 25.196 1.00 20.32 C ATOM 1819 O GLUB2117 32.989 −1.010 26.303 1.00 18.78 O ATOM 1820 N GLU B2118 34.384−2.141 24.931 1.00 22.46 N ATOM 1821 CA GLU B2118 35.413 −2.366 25.9491.00 26.31 C ATOM 1822 CB GLU B2118 35.364 −3.830 26.415 1.00 28.48 CATOM 1823 CG GLU B2118 36.185 −4.151 27.657 1.00 31.58 C ATOM 1824 CDGLU B2118 35.479 −3.793 28.952 1.00 33.18 C ATOM 1825 OE1 GLU B211834.479 −4.464 29.295 1.00 34.62 O ATOM 1826 OE2 GLU B2118 35.925 −2.83929.628 1.00 34.75 O ATOM 1827 C GLU B2118 36.820 −2.039 25.435 1.0027.70 C ATOM 1828 O GLU B2118 36.958 −1.559 24.285 1.00 28.17 O ATOM1829 OXT GLU B2118 37.784 −2.267 26.199 1.00 29.81 O TER 1830 GLU B2118ATOM 1831 CB MET C3003 38.407 0.566 12.507 1.00 29.11 C ATOM 1832 CG METC3003 38.953 −0.372 11.436 1.00 32.10 C ATOM 1833 SD MET C3003 39.9710.467 10.186 1.00 36.76 S ATOM 1834 CE MET C3003 41.535 0.656 11.0781.00 35.20 C ATOM 1835 C MET C3003 36.229 −0.625 12.723 1.00 24.49 CATOM 1836 O MET C3003 36.251 −1.743 12.216 1.00 24.23 O ATOM 1837 N METC3003 38.104 −1.203 14.236 1.00 26.20 N ATOM 1838 CA MET C3003 37.432−0.097 13.493 1.00 26.22 C ATOM 1839 N ILE C3004 35.182 0.190 12.6481.00 22.87 N ATOM 1840 CA ILE C3004 33.960 −0.165 11.933 1.00 21.52 CATOM 1841 CB ILE C3004 32.800 0.781 12.355 1.00 21.32 C ATOM 1842 CG2ILE C3004 31.535 0.469 11.557 1.00 21.05 C ATOM 1843 CG1 ILE C300432.547 0.638 13.864 1.00 20.83 C ATOM 1844 CD1 ILE C3004 31.537 1.61514.443 1.00 20.25 C ATOM 1845 C ILE C3004 34.199 −0.043 10.422 1.0021.57 C ATOM 1846 O ILE C3004 34.938 0.848 9.979 1.00 21.16 O ATOM 1847N VAL C3005 33.610 −0.952 9.638 1.00 20.59 N ATOM 1848 CA VAL C300533.749 −0.906 8.182 1.00 20.63 C ATOM 1849 CB VAL C3005 34.642 −2.0687.628 1.00 21.47 C ATOM 1850 CG1 VAL C3005 36.083 −1.890 8.090 1.0021.00 C ATOM 1851 CG2 VAL C3005 34.109 −3.413 8.076 1.00 23.00 C ATOM1852 C VAL C3005 32.413 −0.901 7.422 1.00 19.52 C ATOM 1853 O VAL C300532.411 −0.880 6.192 1.00 19.11 O ATOM 1854 N GLY C3006 31.289 −0.9068.149 1.00 18.23 N ATOM 1855 CA GLY C3006 29.974 −0.880 7.508 1.00 17.17C ATOM 1856 C GLY C3006 28.797 −0.986 8.482 1.00 16.61 C ATOM 1857 O GLYC3006 28.963 −1.526 9.579 1.00 16.76 O ATOM 1858 N HIS C3007 27.620−0.477 8.093 1.00 15.51 N ATOM 1859 CA HIS C3007 26.400 −0.531 8.9351.00 15.40 C ATOM 1860 CB HIS C3007 26.418 0.624 9.953 1.00 15.15 C ATOM1861 CG HIS C3007 25.191 0.709 10.821 1.00 14.61 C ATOM 1862 C02 HISC3007 24.430 1.772 11.180 1.00 14.84 C ATOM 1863 ND1 HIS C3007 24.668−0.377 11.493 1.00 15.01 N ATOM 1864 CE1 HIS C3007 23.639 0.013 12.2291.00 15.56 C ATOM 1865 NE2 HIS C3007 23.475 1.313 12.058 1.00 15.15 NATOM 1866 C HIS C3007 25.086 −0.476 8.115 1.00 14.78 C ATOM 1867 O HISC3007 24.933 0.372 7.228 1.00 14.49 O ATOM 1868 N GLY C3008 24.145−1.376 8.418 1.00 14.82 N ATOM 1869 CA GLY C3008 22.867 −1.390 7.7091.00 14.90 C ATOM 1870 C GLY C3008 21.668 −1.918 8.495 1.00 15.74 C ATOM1871 O GLY C3008 21.835 −2.757 9.391 1.00 14.75 O ATOM 1872 N ILE C300920.465 −1.425 8.166 1.00 15.25 N ATOM 1873 CA ILE C3009 19.211 −1.8478.823 1.00 15.66 C ATOM 1874 CB ILE C3009 18.692 −0.769 9.837 1.00 14.95C ATOM 1875 CG2 ILE C3009 19.789 −0.421 10.873 1.00 15.05 C ATOM 1876CG1 ILE C3009 18.261 0.492 9.079 1.00 14.33 C ATOM 1877 CD1 ILE C300917.632 1.555 9.956 1.00 14.63 C ATOM 1878 C ILE C3009 18.090 −2.1027.780 1.00 16.20 C ATOM 1879 O ILE C3009 18.221 −1.696 6.619 1.00 16.14O ATOM 1880 N ASP C3010 17.004 −2.762 8.204 1.00 16.80 N ATOM 1881 CAASP C3010 15.853 −3.080 7.330 1.00 17.32 C ATOM 1882 CB ASP C3010 16.130−4.365 6.527 1.00 18.68 C ATOM 1883 CG ASP C3010 14.977 −4.741 5.5791.00 18.99 C ATOM 1884 OD1 ASP C3010 14.852 −4.105 4.518 1.00 19.45 OATOM 1885 OD2 ASP C3010 14.193 −5.667 5.896 1.00 19.42 O ATOM 1886 C ASPC3010 14.549 −3.290 8.120 1.00 18.11 C ATOM 1887 O ASP C3010 14.580−3.711 9.283 1.00 17.23 O ATOM 1888 N ILE C3011 13.411 −2.978 7.488 1.0017.97 N ATOM 1889 CA ILE C3011 12.082 −3.191 8.081 1.00 18.54 C ATOM1890 CB ILE C3011 11.444 −1.876 8.656 1.00 18.66 C ATOM 1891 CG2 ILEC3011 11.363 −0.776 7.579 1.00 19.04 C ATOM 1892 CG1 ILE C3011 10.048−2.185 9.211 1.00 19.19 C ATOM 1893 CG1 ILE C3011 9.421 −1.049 9.9991.00 19.08 C ATOM 1894 C ILE C3011 11.207 −3.762 6.950 1.00 18.75 C ATOM1895 O ILE C3011 11.286 −3.288 5.825 1.00 18.39 O ATOM 1896 N GLU C301210.389 −4.774 7.253 1.00 19.66 N ATOM 1897 CA GLU C3012 9.544 −5.4336.246 1.00 20.80 C ATOM 1898 CB GLU C3012 10.290 −6.663 5.706 1.00 22.15C ATOM 1899 CG GLU C3012 9.468 −7.566 4.774 1.00 23.49 C ATOM 1900 CDGLU C3012 9.692 −7.274 3.300 1.00 24.70 C ATOM 1901 OE1 GLU C3012 10.294−6.228 2.973 1.00 24.77 O ATOM 1902 OE2 GLU C3012 9.258 −8.095 2.4601.00 25.50 O ATOM 1903 C GLU C3012 8.160 −5.870 6.759 1.00 21.36 C ATOM1904 O GLU C3012 8.049 −6.431 7.848 1.00 20.37 O ATOM 1905 N GLU C30137.111 −5.614 5.971 1.00 22.03 N ATOM 1906 CA GLU C3013 5.743 −6.0046.345 1.00 23.43 C ATOM 1907 CB GLU C3013 4.703 −5.207 5.534 1.00 24.60C ATOM 1908 CG GLU C3013 4.706 −3.683 5.716 1.00 26.52 C ATOM 1909 CDGLU C3013 4.063 −3.212 7.018 1.00 28.49 C ATOM 1910 OE1 GLU C3013 3.071−3.834 7.467 1.00 28.55 O ATOM 1911 OE2 GLU C3013 4.533 −2.192 7.5791.00 28.72 O ATOM 1912 C GLU C3013 5.517 −7.501 6.075 1.00 23.35 C ATOM1913 O GLU C3013 5.931 −8.012 5.032 1.00 23.44 O ATOM 1914 N LEU C30144.855 −8.198 7.000 1.00 23.78 N ATOM 1915 CA LEU C3014 4.578 −9.6276.818 1.00 24.31 C ATOM 1916 CB LEU C3014 3.922 −10.227 8.071 1.00 24.95C ATOM 1917 CG LEU C3014 4.664 −10.149 9.417 1.00 27.00 C ATOM 1918 CD1LEU C3014 3.957 −11.044 10.423 1.00 27.46 C ATOM 1919 CD2 LEU C30146.118 −10.589 9.258 1.00 26.69 C ATOM 1920 C LEU C3014 3.660 −9.8675.608 1.00 24.29 C ATOM 1921 O LEU C3014 3.680 −10.939 5.004 1.00 23.68O ATOM 1922 N ALA C3015 2.857 −8.868 5.262 1.00 24.50 N ATOM 1923 CA ALAC3015 1.946 −8.984 4.120 1.00 24.91 C ATOM 1924 CB ALA C3015 1.082−7.732 4.016 1.00 25.04 C ATOM 1925 C ALA C3015 2.691 −9.220 2.803 1.0025.57 C ATOM 1926 O ALA C3015 2.215 −9.962 1.940 1.00 25.88 O ATOM 1927N SER C3016 3.857 −8.592 2.648 1.00 25.61 N ATOM 1928 CA SER C3016 4.658−8.737 1.432 1.00 25.91 C ATOM 1929 CB SER C3016 5.829 −7.742 1.441 1.0026.86 C ATOM 1930 OG SER C3016 5.385 −6.401 1.589 1.00 27.09 O ATOM 1931C SER C3016 5.204 −10.159 1.275 1.00 26.38 C ATOM 1932 O SER C3016 5.276−10.690 0.161 1.00 25.43 O ATOM 1933 N ILE C3017 5.603 −10.768 2.3901.00 26.46 N ATOM 1934 CA ILE C3017 6.128 −12.131 2.365 1.00 26.86 CATOM 1935 CB ILE C3017 6.839 −12.474 3.706 1.00 26.57 C ATOM 1936 CG2ILE C3017 7.306 −13.925 3.709 1.00 26.15 C ATOM 1937 CG1 ILE C3017 8.029−11.526 3.923 1.00 26.30 C ATOM 1938 CD1 ILE C3017 9.102 −11.612 2.8421.00 26.29 C ATOM 1939 C ILE C3017 4.986 −13.129 2.121 1.00 28.01 C ATOM1940 O ILE C3017 5.160 −14.133 1.426 1.00 27.90 O ATOM 1941 N GLU C30183.816 −12.837 2.679 1.00 28.89 N ATOM 1942 CA GLU C3018 2.657 −13.7132.530 1.00 30.68 C ATOM 1943 CB GLU C3018 1.527 −13.250 3.456 1.00 31.08C ATOM 1944 CG GLU C3018 1.936 −13.180 4.919 1.00 32.50 C ATOM 1945 CDGLU C3018 0.853 −12.614 5.817 1.00 33.07 C ATOM 1946 OE1 GLU C3018 0.161−11.663 5.395 1.00 33.76 O ATOM 1947 OE2 GLU C3018 0.704 −13.108 6.9551.00 33.50 O ATOM 1948 C GLU C3018 2.144 −13.796 1.092 1.00 31.38 C ATOM1949 O GLU C3018 1.736 −14.868 0.639 1.00 31.29 O ATOM 1950 N SER C30192.166 −12.677 0.372 1.00 32.24 N ATOM 1951 CA SER C3019 1.691 −12.676−1.008 1.00 33.36 C ATOM 1952 CB SER C3019 1.420 −11.240 −1.494 1.0033.64 C ATOM 1953 OG SER C3019 2.610 −10.547 −1.838 1.00 34.47 O ATOM1954 C SER C3019 2.706 −13.364 −1.918 1.00 34.14 C ATOM 1955 O SER C30192.331 −14.055 −2.864 1.00 34.07 O ATOM 1956 N ALA C3020 3.989 −13.191−1.611 1.00 34.65 N ATOM 1957 CA ALA C3020 5.061 −13.791 −2.399 1.0035.89 C ATOM 1958 CB ALA C3020 6.415 −13.247 −1.938 1.00 35.73 C ATOM1959 C ALA C3020 5.071 −15.322 −2.347 1.00 36.89 C ATOM 1960 O ALA C30205.451 −15.978 −3.317 1.00 36.66 O ATOM 1961 N VAL C3021 4.663 −15.891−1.217 1.00 38.20 N ATOM 1962 CA VAL C3021 4.640 −17.343 −1.078 1.0040.04 C ATOM 1963 CB VAL C3021 4.270 −17.770 0.362 1.00 40.00 C ATOM1964 CG1 VAL C3021 4.180 −19.285 0.445 1.00 40.22 C ATOM 1965 CG2 VALC3021 5.310 −17.255 1.347 1.00 40.17 C ATOM 1966 C VAL C3021 3.636−17.969 −2.043 1.00 41.37 C ATOM 1967 O VAL C3021 3.939 −18.954 −2.7181.00 41.44 O ATOM 1968 N THR C3022 2.443 −17.387 −2.105 1.00 42.72 NATOM 1969 CA THR C3022 1.382 −17.883 −2.974 1.00 44.38 C ATOM 1970 CBTHR C3022 0.049 −17.160 −2.683 1.00 43.84 C ATOM 1971 OG1 THR C3022−0.341 −17.403 −1.326 1.00 43.59 O ATOM 1972 CG2 THR C3022 −1.048−17.665 −3.612 1.00 43.81 C ATOM 1973 C THR C3022 1.703 −17.738 −4.4611.00 45.84 C ATOM 1974 O THR C3022 1.725 −18.730 −5.193 1.00 45.92 OATOM 1975 N ARG C3023 1.951 −16.508 −4.906 1.00 47.48 N ATOM 1976 CA ARGC3023 2.250 −16.253 −6.313 1.00 49.27 C ATOM 1977 CB ARG C3023 2.771−14.823 −6.502 1.00 49.46 C ATOM 1978 CG ARG C3023 2.801 −14.390 −7.9581.00 49.98 C ATOM 1979 CD ARG C3023 2.939 −12.884 −8.125 1.00 50.04 CATOM 1980 NE ARG C3023 4.288 −12.399 −7.854 0.05 50.32 N ATOM 1981 CZARG C3023 4.694 −11.158 −8.105 0.05 50.40 C ATOM 1982 NH1 ARG C30233.853 −10.279 −8.634 0.05 50.48 N ATOM 1983 NH2 ARG C3023 5.940 −10.797−7.833 0.05 50.49 N ATOM 1984 C ARG C3023 3.260 −17.259 −6.861 1.0050.29 C ATOM 1985 O ARG C3023 2.889 −18.186 −7.580 1.00 50.77 O ATOM1986 N HIS C3024 4.532 −17.074 −6.526 1.00 51.47 N ATOM 1987 CA HISC3024 5.581 −17.988 −6.970 1.00 52.39 C ATOM 1988 CB HIS C3024 6.822−17.207 −7.410 0.05 52.53 C ATOM 1989 CG HIS C3024 7.108 −17.304 −8.8760.05 52.72 C ATOM 1990 CD2 HIS C3024 7.177 −16.353 −9.838 0.05 52.78 CATOM 1991 ND1 HIS C3024 7.367 −18.503 −9.505 0.05 52.78 N ATOM 1992 CE1HIS C3024 7.583 −18.287 −10.790 0.05 52.83 C ATOM 1993 NE2 HIS C30247.474 −16.990 −11.018 0.05 52.83 N ATOM 1994 C HIS C3024 5.931 −18.911−5.806 1.00 53.02 C ATOM 1995 O HIS C3024 6.822 −18.613 −5.013 1.0052.97 O ATOM 1996 N GLU C3025 5.222 −20.032 −5.712 1.00 53.71 N ATOM1997 CA GLU C3025 5.430 −20.992 −4.632 1.00 54.23 C ATOM 1998 CB GLUC3025 4.308 −22.035 −4.647 1.00 55.24 C ATOM 1999 CG GLU C3025 4.150−22.772 −5.965 1.00 56.63 C ATOM 2000 CD GLU C3025 2.869 −23.585 −6.0241.00 57.48 C ATOM 2001 OE1 GLU C3025 2.657 −24.435 −5.131 1.00 58.10 OATOM 2002 OE2 GLU C3025 2.075 −23.372 −6.966 1.00 57.87 O ATOM 2003 CGLU C3025 6.796 −21.684 −4.626 1.00 53.75 C ATOM 2004 O GLU C3025 6.916−22.841 −4.227 1.00 53.95 O ATOM 2005 N GLY C3026 7.820 −20.961 −5.0681.00 53.15 N ATOM 2006 CA GLY C3026 9.171 −21.492 −5.080 1.00 51.80 CATOM 2007 C GLY C3026 10.057 −20.503 −4.340 1.00 50.97 C ATOM 2008 O GLYC3026 11.260 −20.712 −4.167 1.00 50.85 O ATOM 2009 N PHE C3027 9.426−19.418 −3.899 1.00 49.86 N ATOM 2010 CA PHE C3027 10.077 −18.331 −3.1731.00 48.78 C ATOM 2011 CB PHE C3027 9.001 −17.419 −2.570 1.00 48.81 CATOM 2012 CG PHE C3027 9.546 −16.198 −1.884 1.00 48.66 C ATOM 2013 CD1PHE C3027 10.279 −15.252 −2.593 1.00 48.61 C ATOM 2014 CD2 PHE C30279.313 −15.986 −0.527 1.00 48.69 C ATOM 2015 CE1 PHE C3027 10.772 −14.111−1.962 1.00 48.58 C ATOM 2016 CE2 PHE C3027 9.802 −14.849 0.113 1.0048.35 C ATOM 2017 CZ PHE C3027 10.533 −13.910 −0.606 1.00 48.38 C ATOM2018 C PHE C3027 11.037 −18.795 −2.076 1.00 47.88 C ATOM 2019 O PHEC3027 12.188 −18.364 −2.027 1.00 47.77 O ATOM 2020 N ALA C3028 10.558−19.676 −1.205 1.00 47.03 N ATOM 2021 CA ALA C3028 11.362 −20.186 −0.0971.00 46.36 C ATOM 2022 CB ALA C3028 10.529 −21.147 0.741 1.00 46.30 CATOM 2023 C ALA C3028 12.668 −20.862 −0.519 1.00 45.98 C ATOM 2024 O ALAC3028 13.735 −20.562 0.026 1.00 46.02 O ATOM 2025 N LYS C3029 12.585−21.774 −1.483 1.00 44.97 N ATOM 2026 CA LYS C3029 13.762 −22.497 −1.9521.00 44.02 C ATOM 2027 CB LYS C3029 13.377 −23.478 −3.065 1.00 44.26 CATOM 2028 CG LYS C3029 12.440 −24.589 −2.621 0.05 44.27 C ATOM 2029 CDLYS C3029 12.186 −25.576 −3.749 0.05 44.38 C ATOM 2030 CE LYS C302911.290 −26.717 −3.296 0.05 44.42 C ATOM 2031 NZ LYS C3029 11.066 −27.712−4.380 0.05 44.48 N ATOM 2032 C LYS C3029 14.878 −21.586 −2.444 1.0043.30 C ATOM 2033 O LYS C3029 16.055 −21.926 −2.330 1.00 43.66 O ATOM2034 N ARG C3030 14.516 −20.429 −2.988 1.00 42.33 N ATOM 2035 CA ARGC3030 15.515 −19.498 −3.495 1.00 41.38 C ATOM 2036 CB ARG C3030 14.933−18.685 −4.655 1.00 41.73 C ATOM 2037 CG ARG C3030 14.577 −19.527 −5.8700.05 41.77 C ATOM 2038 CD ARG C3030 14.062 −18.672 −7.016 0.05 41.90 CATOM 2039 NE ARG C3030 13.773 −19.474 −8.202 0.05 42.00 N ATOM 2040 CZARG C3030 13.329 −18.977 −9.351 0.05 42.04 C ATOM 2041 NH1 ARG C303013.092 −19.784 −10.377 0.05 42.08 N ATOM 2042 NH2 ARG C3030 13.119−17.674 −9.476 0.05 42.08 N ATOM 2043 C ARG C3030 16.073 −18.551 −2.4351.00 40.66 C ATOM 2044 O ARG C3030 17.141 −17.969 −2.620 1.00 40.56 OATOM 2045 N VAL C3031 15.357 −18.402 −1.324 1.00 39.61 N ATOM 2046 CAVAL C3031 15.797 −17.509 −0.252 1.00 38.51 C ATOM 2047 CB VAL C303114.593 −16.737 0.354 1.00 38.68 C ATOM 2048 CG1 VAL C3031 15.046 −15.8991.545 1.00 39.01 C ATOM 2049 CG2 VAL C3031 13.964 −15.843 −0.703 1.0039.32 C ATOM 2050 C VAL C3031 16.535 −18.222 0.887 1.00 37.22 C ATOM2051 O VAL C3031 17.392 −17.625 1.540 1.00 36.96 O ATOM 2052 N LEU C303216.215 −19.494 1.109 1.00 35.97 N ATOM 2053 CA LEU C3032 16.825 −20.2682.194 1.00 35.20 C ATOM 2054 CB LEU C3032 15.713 −20.865 3.062 1.0034.43 C ATOM 2055 CG LEU C3032 14.682 −19.887 3.635 1.00 34.07 C ATOM2056 CD1 LEU C3032 13.508 −20.658 4.224 1.00 34.12 C ATOM 2057 CD2 LEUC3032 15.340 −19.010 4.694 1.00 33.54 C ATOM 2058 C LEU C3032 17.774−21.395 1.756 1.00 35.04 C ATOM 2059 O LEU C3032 17.592 −21.997 0.6961.00 34.60 O ATOM 2060 N THR C3033 18.780 −21.679 2.584 1.00 34.45 NATOM 2061 CA THR C3033 19.729 −22.755 2.293 1.00 34.22 C ATOM 2062 CBTHR C3033 21.050 −22.619 3.096 1.00 33.96 C ATOM 2063 OG1 THR C303320.797 −22.889 4.481 1.00 33.02 O ATOM 2064 CG2 THR C3033 21.630 −21.2222.953 1.00 34.21 C ATOM 2065 C THR C3033 19.063 −24.063 2.720 1.00 34.16C ATOM 2066 O THR C3033 17.968 −24.052 3.279 1.00 33.78 O ATOM 2067 NALA C3034 19.729 −25.185 2.472 1.00 34.40 N ATOM 2068 CA ALA C303419.178 −26.487 2.839 1.00 34.48 C ATOM 2069 CB ALA C3034 20.103 −27.5982.350 1.00 34.65 C ATOM 2070 C ALA C3034 18.927 −26.638 4.341 1.00 34.51C ATOM 2071 O ALA C3034 17.867 −27.117 4.751 1.00 34.56 O ATOM 2072 NLEU C3035 19.895 −26.233 5.162 1.00 34.52 N ATOM 2073 CA LEU C303519.755 −26.345 6.612 1.00 34.61 C ATOM 2074 CB LEU C3035 21.087 −26.0477.308 1.00 34.52 C ATOM 2075 CG LEU C3035 21.101 −26.182 8.834 0.0534.52 C ATOM 2076 CD1 LEU C3035 20.741 −27.607 9.228 0.05 34.51 C ATOM2077 CD2 LEU C3035 22.475 −25.814 9.369 0.05 34.53 C ATOM 2078 C LEUC3035 18.675 −25.414 7.156 1.00 35.00 C ATOM 2079 O LEU C3035 17.965−25.769 8.098 1.00 35.04 O ATOM 2080 N GLU C3036 18.558 −24.222 6.5741.00 35.33 N ATOM 2081 CA GLU C3036 17.537 −23.263 7.004 1.00 35.62 CATOM 2082 CB GLU C3036 17.741 −21.907 6.310 1.00 34.70 C ATOM 2083 CGGLU C3036 18.809 −21.006 6.941 1.00 33.21 C ATOM 2084 CD GLU C303619.117 −19.767 6.103 1.00 32.82 C ATOM 2085 OE1 GLU C3036 19.598 −18.7596.671 1.00 31.24 O ATOM 2086 OE2 GLU C3036 18.893 −19.803 4.873 1.0032.21 O ATOM 2087 C GLU C3036 16.155 −23.815 6.654 1.00 36.75 C ATOM2088 O GLU C3036 15.205 −23.687 7.427 1.00 36.40 O ATOM 2089 N MET C303716.064 −24.436 5.481 1.00 38.24 N ATOM 2090 CA MET C3037 14.821 −25.0184.981 1.00 40.09 C ATOM 2091 CB MET C3037 15.064 −25.625 3.596 1.0041.14 C ATOM 2092 CG MET C3037 13.808 −26.028 2.834 1.00 43.15 C ATOM2093 SD MET C3037 12.851 −24.618 2.239 1.00 45.06 S ATOM 2094 CE METC3037 11.189 −25.242 2.400 1.00 44.92 C ATOM 2095 C MET C3037 14.270−26.089 5.926 1.00 40.63 C ATOM 2096 O MET C3037 13.061 −26.171 6.1511.00 40.94 O ATOM 2097 N GLU C3038 15.159 −26.911 6.473 1.00 41.23 NATOM 2098 CA GLU C3038 14.752 −27.969 7.393 1.00 41.49 C ATOM 2099 CBGLU C3038 15.982 −28.713 7.924 1.00 41.61 C ATOM 2100 CG GLU C303816.711 −29.544 6.878 0.05 41.50 C ATOM 2101 CD GLU C3038 15.889 −30.7216.385 0.05 41.51 C ATOM 2102 OE1 GLU C3038 16.376 −31.459 5.503 0.0541.48 O ATOM 2103 OE2 GLU C3038 14.758 −30.911 6.880 0.05 41.45 O ATOM2104 C GLU C3038 13.958 −27.391 8.559 1.00 41.78 C ATOM 2105 O GLU C303812.984 −27.989 9.013 1.00 41.81 O ATOM 2106 N ARG C3039 14.384 −26.2269.037 1.00 42.11 N ATOM 2107 CA ARG C3039 13.716 −25.550 10.146 1.0042.69 C ATOM 2108 CB ARG C3039 14.580 −24.380 10.634 1.00 43.67 C ATOM2109 CG ARG C3039 13.950 −23.514 11.722 1.00 45.06 C ATOM 2110 CD ARGC3039 13.752 −24.276 13.026 1.00 46.69 C ATOM 2111 NE ARG C3039 13.295−23.394 14.099 1.00 47.90 N ATOM 2112 CZ ARG C3039 12.966 −23.803 15.3211.00 48.72 C ATOM 2113 NH1 ARG C3039 13.040 −25.089 15.637 1.00 49.17 NATOM 2114 NH2 ARG C3039 12.563 −22.925 16.230 1.00 49.02 N ATOM 2115 CARG C3039 12.343 −25.034 9.714 1.00 42.44 C ATOM 2116 O ARG C3039 11.360−25.153 10.448 1.00 42.21 O ATOM 2117 N PHE C3040 12.293 −24.467 8.5121.00 42.44 N ATOM 2118 CA PHE C3040 11.064 −23.909 7.948 1.00 42.58 CATOM 2119 CB PHE C3040 11.343 −23.394 6.529 1.00 41.84 C ATOM 2120 CGPHE C3040 10.165 −22.713 5.879 1.00 41.26 C ATOM 2121 CD1 PHE C30409.621 −21.556 6.428 1.00 40.76 C ATOM 2122 CD2 PHE C3040 9.610 −23.2234.708 1.00 40.96 C ATOM 2123 CE1 PHE C3040 8.541 −20.915 5.821 1.0040.74 C ATOM 2124 CE2 PHE C3040 8.527 −22.590 4.090 1.00 40.92 C ATOM2125 CZ PHE C3040 7.992 −21.433 4.649 1.00 40.88 C ATOM 2126 C PHE C30409.899 −24.902 7.913 1.00 43.12 C ATOM 2127 O PHE C3040 8.790 −24.5858.343 1.00 42.92 O ATOM 2128 N THR C3041 10.156 −26.104 7.406 1.00 43.77N ATOM 2129 CA THR C3041 9.119 −27.126 7.303 1.00 44.43 C ATOM 2130 CBTHR C3041 9.569 −22.283 6.395 1.00 44.80 C ATOM 2131 OG1 THR C304110.703 −28.936 6.978 1.00 45.05 O ATOM 2132 CG2 THR C3041 9.935 −27.7595.016 1.00 45.00 C ATOM 2133 C THR C3041 8.676 −27.719 8.635 1.00 44.57C ATOM 2134 O THR C3041 7.611 −28.327 8.721 1.00 44.92 O ATOM 2135 N SERC3042 9.488 −27.548 9.672 1.00 44.91 N ATOM 2136 CA SER C3042 9.160−28.091 10.986 1.00 44.98 C ATOM 2137 CB SER C3042 10.439 −28.297 11.8011.00 45.18 C ATOM 2138 OG SER C3042 11.336 −29.151 11.110 1.00 45.91 OATOM 2139 C SER C3042 8.194 −27.212 11.770 1.00 44.99 C ATOM 2140 O SERC3042 7.536 −27.683 12.699 1.00 45.11 O ATOM 2141 N LEU C3043 8.112−25.938 11.397 1.00 44.68 N ATOM 2142 CA LEU C3043 7.228 −24.993 12.0731.00 44.47 C ATOM 2143 CB LEU C3043 7.882 −23.608 12.124 1.00 44.33 CATOM 2144 CG LEU C3043 9.250 −23.485 12.797 1.00 44.21 C ATOM 2145 CD1LEU C3043 9.761 −22.052 12.662 1.00 44.22 C ATOM 2146 CD2 LEU C30439.139 −23.875 14.265 1.00 44.47 C ATOM 2147 C LEU C3043 5.888 −24.89911.347 1.00 44.31 C ATOM 2148 O LEU C3043 5.738 −25.422 10.240 1.0044.09 O ATOM 2149 N LYS C3044 4.923 −24.221 11.965 1.00 44.27 N ATOM2150 CA LYS C3044 3.601 −24.064 11.365 1.00 44.15 C ATOM 2151 CB LYSC3044 2.703 −25.234 11.777 1.00 45.11 C ATOM 2152 CG LYS C3044 1.429−25.375 10.953 1.00 46.10 C ATOM 2153 CD LYS C3044 0.462 −26.398 11.5471.00 47.10 C ATOM 2154 CE LYS C3044 1.099 −27.774 11.701 1.00 47.88 CATOM 2155 NZ LYS C3044 2.155 −27.802 12.758 1.00 48.36 N ATOM 2156 C LYSC3044 2.924 −22.745 11.753 1.00 43.58 C ATOM 2157 O LYS C3044 3.349−22.062 12.687 1.00 43.58 O ATOM 2158 N GLY C3045 1.868 −22.397 11.0221.00 42.72 N ATOM 2159 CA GLY C3045 1.129 −21.177 11.299 1.00 41.65 CATOM 2160 C GLY C3045 1.932 −19.893 11.197 1.00 40.64 C ATOM 2161 O GLYC3045 2.788 −19.749 10.323 1.00 40.57 O ATOM 2162 N ARG C3046 1.644−18.956 12.097 1.00 39.78 N ATOM 2163 CA ARG C3046 2.327 −17.666 12.1291.00 38.64 C ATOM 2164 CB ARG C3046 1.752 −16.792 13.249 1.00 38.93 CATOM 2165 CG ARG C3046 2.393 −15.415 13.350 0.05 38.89 C ATOM 2166 CDARG C3046 1.769 −14.591 14.465 0.05 38.99 C ATOM 2167 NE ARG C3046 0.346−14.352 14.241 0.05 39.04 N ATOM 2168 CZ ARG C3046 −0.428 −13.636 15.0500.05 39.08 C ATOM 2169 NH1 ARG C3046 −1.713 −13.471 14.768 0.05 39.09 NATOM 2170 NH2 ARG C3046 0.084 −13.084 16.142 0.05 39.12 N ATOM 2171 CARG C3046 3.826 −17.840 12.338 1.00 37.81 C ATOM 2172 O ARG C3046 4.629−17.130 11.735 1.00 37.34 O ATOM 2173 N ARG C3047 4.195 −18.785 13.1981.00 36.94 N ATOM 2174 CA ARG C3047 5.601 −19.056 13.485 1.00 35.80 CATOM 2175 CB ARG C3047 5.727 −20.255 14.424 1.00 37.34 C ATOM 2176 CGARG C3047 5.554 −19.924 15.887 1.00 38.72 C ATOM 2177 CD ARG C3047 5.695−21.177 16.731 1.00 40.55 C ATOM 2178 NE ARG C3047 6.145 −20.870 18.0831.00 41.86 N ATOM 2179 CZ ARG C3047 7.328 −20.335 18.369 1.00 42.33 CATOM 2180 NH1 ARG C3047 8.181 −20.050 17.395 1.00 43.10 N ATOM 2181 NH2ARG C3047 7.659 −20.087 19.629 1.00 42.88 N ATOM 2182 C ARG C3047 6.408−19.329 12.223 1.00 34.36 C ATOM 2183 O ARG C3047 7.518 −18.812 12.0571.00 33.67 O ATOM 2184 N GLN C3048 5.852 −20.152 11.340 1.00 32.32 NATOM 2185 CA GLN C3048 6.522 −20.493 10.095 1.00 30.19 C ATOM 2186 CBGLN C3048 5.709 −21.538 9.326 1.00 30.56 C ATOM 2187 CG GLN C3048 6.346−21.947 8.010 1.00 31.08 C ATOM 2188 CD GLN C3048 5.545 −22.989 7.2561.00 31.55 C ATOM 2189 OE1 GLN C3048 4.363 −22.793 6.971 1.00 32.61 OATOM 2190 NE2 GLN C3048 6.189 −24.100 6.919 1.00 31.23 N ATOM 2191 C GLNC3048 6.749 −19.266 9.211 1.00 28.78 C ATOM 2192 O GLN C3048 7.816−19.113 8.615 1.00 27.77 O ATOM 2193 N ILE C3049 5.747 −18.396 9.1241.00 27.16 N ATOM 2194 CA ILE C3049 5.862 −17.195 8.298 1.00 26.51 CATOM 2195 CB ILE C3049 4.485 −16.521 8.086 1.00 26.30 C ATOM 2196 CG2ILE C3049 4.647 −15.250 7.255 1.00 26.17 C ATOM 2197 CG1 ILE C3049 3.530−17.491 7.380 1.00 26.22 C ATOM 2198 CD1 ILE C3049 4.023 −17.978 6.0141.00 26.61 C ATOM 2199 C ILE C3049 6.831 −16.178 8.910 1.00 25.94 C ATOM2200 O ILE C3049 7.570 −15.510 8.192 1.00 25.27 O ATOM 2201 N GLU C30506.824 −16.069 10.236 1.00 26.02 N ATOM 2202 CA GLU C3050 7.716 −15.14110.935 1.00 25.96 C ATOM 2203 CB GLU C3050 7.347 −15.075 12.423 1.0027.39 C ATOM 2204 CG GLU C3050 6.073 −14.287 12.724 1.00 29.92 C ATOM2205 CD GLU C3050 6.345 −12.853 13.175 1.00 31.52 C ATOM 2206 OE1 GLUC3050 7.446 −12.322 12.894 1.00 32.57 O ATOM 2207 OE2 GLU C3050 5.444−12.252 13.802 1.00 31.86 O ATOM 2208 C GLU C3050 9.195 −15.521 10.7921.00 24.88 C ATOM 2209 O GLU C3050 10.061 −14.650 10.815 1.00 24.17 OATOM 2210 N TYR C3051 9.481 −16.815 10.652 1.00 23.54 N ATOM 2211 CA TYRC3051 10.863 −17.281 10.508 1.00 22.59 C ATOM 2212 CB TYR C3051 10.941−18.808 10.711 1.00 23.12 C ATOM 2213 CG TYR C3051 12.317 −19.425 10.4731.00 23.17 C ATOM 2214 CD1 TYR C3051 12.685 −19.902 9.213 1.00 23.85 CATOM 2215 CE1 TYR C3051 13.954 −20.454 8.984 1.00 24.32 C ATOM 2216 CD2TYR C3051 13.253 −19.515 11.504 1.00 24.30 C ATOM 2217 CE2 TYR C305114.528 −20.064 11.288 1.00 24.54 C ATOM 2218 CZ TYR C3051 14.868 −20.52810.026 1.00 24.99 C ATOM 2219 OH TYR C3051 16.122 −21.050 9.803 1.0025.78 O ATOM 2220 C TYR C3051 11.419 −16.894 9.140 1.00 22.18 C ATOM2221 O TYR C3051 12.546 −16.395 9.031 1.00 20.97 O ATOM 2222 N LEU C305210.618 −17.115 8.101 1.00 21.39 N ATOM 2223 CA LEU C3052 11.016 −16.7876.736 1.00 21.55 C ATOM 2224 CB LEU C3052 9.935 −17.254 5.747 1.00 22.13C ATOM 2225 CG LEU C3052 10.124 −16.929 4.259 1.00 21.93 C ATOM 2226 CD1LEU C3052 11.439 −17.515 3.755 1.00 22.55 C ATOM 2227 CD2 LEU C30528.958 −17.495 3.469 1.00 22.75 C ATOM 2228 C LEU C3052 11.245 −15.2846.574 1.00 21.31 C ATOM 2229 O LEU C3052 12.196 −14.866 5.914 1.00 21.85O ATOM 2230 N ALA C3053 10.371 −14.484 7.181 1.00 20.68 N ATOM 2231 CAALA C3053 10.454 −13.025 7.102 1.00 20.75 C ATOM 2232 CB ALA C3053 9.203−12.401 7.738 1.00 20.99 C ATOM 2233 C ALA C3053 11.720 −12.469 7.7681.00 20.60 C ATOM 2234 O ALA C3053 12.356 −11.552 7.237 1.00 20.36 OATOM 2235 N GLY C3054 12.073 −13.027 8.925 1.00 20.45 N ATOM 2236 CA GLYC3054 13.264 −12.597 9.646 1.00 20.63 C ATOM 2237 C GLY C3054 14.576−12.928 8.945 1.00 20.53 C ATOM 2238 O GLY C3054 15.550 −12.174 9.0341.00 19.61 O ATOM 2239 N ARG C3055 14.620 −14.065 8.256 1.00 20.88 NATOM 2240 CA ARG C3055 15.824 −14.457 7.527 1.00 21.09 C ATOM 2241 CBARG C3055 15.731 −15.930 7.101 1.00 21.81 C ATOM 2242 CG ARG C305516.533 −16.895 7.988 1.00 23.24 C ATOM 2243 CD ARG C3055 16.139 −16.8019.465 1.00 23.82 C ATOM 2244 NE ARG C3055 17.018 −17.600 10.325 1.0023.91 N ATOM 2245 CZ ARG C3055 16.881 −17.706 11.646 1.00 24.64 C ATOM2246 NH1 ARG C3055 15.901 −17.065 12.267 1.00 23.93 N ATOM 2247 NH2 ARGC3055 17.719 −18.459 12.352 1.00 25.21 N ATOM 2248 C ARG C3055 16.017−13.552 6.301 1.00 21.23 C ATOM 2249 O ARG C3055 17.142 −13.234 5.9211.00 20.84 O ATOM 2250 N TRP C3056 14.911 −13.132 5.694 1.00 21.62 NATOM 2251 CA TRP C3056 14.958 −12.247 4.529 1.00 22.92 C ATOM 2252 CBTRP C3056 13.559 −12.121 3.910 1.00 25.18 C ATOM 2253 CG TRP C305613.515 −11.388 2.594 1.00 27.65 C ATOM 2254 CD2 TRP C3056 13.357 −9.9772.401 1.00 28.51 C ATOM 2255 CE2 TRP C3056 13.413 −9.736 1.009 1.0029.11 C ATOM 2256 CE3 TRP C3056 13.176 −8.892 3.269 1.00 29.11 C ATOM2257 CD1 TRP C3056 13.656 −11.931 1.344 1.00 28.78 C ATOM 2258 NE1 TRPC3056 13.596 −10.944 0.388 1.00 29.88 N ATOM 2259 CZ2 TRP C3056 13.296−8.453 0.465 1.00 28.95 C ATOM 2260 CZ3 TRP C3056 13.060 −7.614 2.7261.00 29.68 C ATOM 2261 CH2 TRP C3056 13.121 −7.409 1.336 1.00 29.31 CATOM 2262 C TRP C3056 15.453 −10.855 4.953 1.00 22.17 C ATOM 2263 O TRPC3056 16.286 −10.247 4.281 1.00 22.33 O ATOM 2264 N SER C3057 14.942−10.365 6.078 1.00 21.01 N ATOM 2265 CA SER C3057 15.311 −9.041 6.5871.00 20.66 C ATOM 2266 CB SER C3057 14.388 −8.663 7.751 1.00 21.23 CATOM 2267 OG SER C3057 14.569 −7.311 8.147 1.00 22.78 O ATOM 2268 C SERC3057 16.786 −8.969 7.025 1.00 20.18 C ATOM 2269 O SER C3057 17.464−7.959 6.803 1.00 19.84 O ATOM 2270 N ALA C3058 17.280 −10.043 7.6331.00 18.66 N ATOM 2271 CA ALA C3058 18.671 −10.090 8.085 1.00 18.83 CATOM 2272 CB ALA C3058 18.905 −11.344 8.939 1.00 17.30 C ATOM 2273 C ALAC3058 19.663 −10.062 6.915 1.00 18.44 C ATOM 2274 O ALA C3058 20.693−9.381 6.980 1.00 18.07 O ATOM 2275 N LYS C3059 19.359 −10.803 5.8511.00 18.60 N ATOM 2276 CA LYS C3059 20.252 −10.850 4.692 1.00 18.76 CATOM 2277 CB LYS C3059 19.848 −12.012 3.766 1.00 18.60 C ATOM 2278 CGLYS C3059 19.956 −13.396 4.447 1.00 18.86 C ATOM 2279 CD LYS C305919.739 −14.578 3.494 1.00 19.28 C ATOM 2280 CE LYS C3059 19.815 −15.9204.244 1.00 20.00 C ATOM 2281 NZ LYS C3059 19.590 −17.130 3.388 1.0020.93 N ATOM 2282 C LYS C3059 20.274 −9.508 3.938 1.00 19.50 C ATOM 2283O LYS C3059 21.306 −9.117 3.388 1.00 20.13 O ATOM 2284 N GLU C306019.142 −8.804 3.935 1.00 20.20 N ATOM 2285 CA GLU C3060 19.026 −7.5013.277 1.00 20.95 C ATOM 2286 CB GLU C3060 17.550 −7.090 3.205 1.00 23.10C ATOM 2287 CG GLU C3060 17.268 −5.738 2.545 1.00 26.69 C ATOM 2288 CDGLU C3060 17.579 −5.717 1.055 1.00 29.57 C ATOM 2289 OE1 GLU C306017.161 −6.660 0.341 1.00 30.70 O ATOM 2290 OE2 GLU C3060 18.232 −4.7490.598 1.00 31.10 O ATOM 2291 C GLU C3060 19.837 −6.432 4.030 1.00 20.53C ATOM 2292 O GLU C3060 20.455 −5.563 3.414 1.00 20.28 O ATOM 2293 N ALAC3061 19.838 −6.497 5.360 1.00 19.74 N ATOM 2294 CA ALA C3061 20.591−5.531 6.165 1.00 19.24 C ATOM 2295 CB ALA C3061 20.252 −5.696 7.6561.00 19.62 C ATOM 2296 C ALA C3061 22.097 −5.711 5.938 1.00 18.92 C ATOM2297 O ALA C3061 22.848 −4.732 5.885 1.00 18.37 O ATOM 2298 N PHE C306222.530 −6.963 5.811 1.00 18.75 N ATOM 2299 CA PHE C3062 23.941 −7.2705.570 1.00 19.65 C ATOM 2300 CB PHE C3062 24.190 −8.783 5.714 1.00 19.70C ATOM 2301 CG PHE C3062 25.592 −9.224 5.325 1.00 20.12 C ATOM 2302 CD1PHE C3062 25.917 −9.472 3.988 1.00 20.55 C ATOM 2303 CD2 PHE C306226.577 −9.391 6.293 1.00 20.19 C ATOM 2304 CE1 PHE C3062 27.200 −9.8833.622 1.00 21.03 C ATOM 2305 CE2 PHE C3062 27.871 −9.803 5.940 1.0020.44 C ATOM 2306 CZ PHE C3062 28.181 −10.049 4.598 1.00 20.96 C ATOM2307 C PHE C3062 24.381 −6.784 4.182 1.00 20.13 C ATOM 2308 O PHE C306225.474 −6.231 4.037 1.00 20.04 O ATOM 2309 N SER C3063 23.530 −6.9813.174 1.00 21.29 N ATOM 2310 CA SER C3063 23.840 −6.551 1.808 1.00 22.13C ATOM 2311 CB SER C3063 22.727 −6.967 0.832 1.00 22.59 C ATOM 2312 OGSER C3063 22.699 −8.374 0.636 1.00 24.36 O ATOM 2313 C SER C3063 24.019−5.032 1.762 1.00 22.61 C ATOM 2314 O SER C3063 24.913 −4.527 1.082 1.0022.10 O ATOM 2315 N LYS C3064 23.160 −4.309 2.477 1.00 22.80 N ATOM 2316CA LYS C3064 23.257 −2.852 2.530 1.00 24.07 C ATOM 2317 CB LYS C306422.013 −2.261 3.210 1.00 23.92 C ATOM 2318 CG LYS C3064 20.734 −2.3762.377 1.00 23.95 C ATOM 2319 CD LYS C3064 19.505 −1.886 3.138 1.00 24.12C ATOM 2320 CE LYS C3064 19.616 −0.407 3.519 1.00 24.30 C ATOM 2321 NZLYS C3064 18.388 0.060 4.209 1.00 24.43 N ATOM 2322 C LYS C3064 24.519−2.408 3.281 1.00 24.84 C ATOM 2323 O LYS C3064 25.132 −1.401 2.939 1.0024.90 O ATOM 2324 N ALA C3065 24.916 −3.166 4.297 1.00 26.22 N ATOM 2325CA ALA C3065 26.101 −2.818 5.079 1.00 28.20 C ATOM 2326 CB ALA C306526.184 −3.693 6.324 1.00 28.57 C ATOM 2327 C ALA C3065 27.396 −2.9434.277 1.00 30.15 C ATOM 2328 O ALA C3065 28.346 −2.188 4.492 1.00 29.72O ATOM 2329 N MET C3066 27.435 −3.903 3.361 1.00 32.11 N ATOM 2330 CAMET C3066 28.629 −4.113 2.555 1.00 35.57 C ATOM 2331 CB MET C3066 28.706−5.577 2.115 1.00 36.03 C ATOM 2332 CG MET C3066 30.087 −5.993 1.6351.00 38.01 C ATOM 2333 SD MET C3066 30.589 −7.586 2.315 1.00 39.43 SATOM 2334 CE MET C3066 29.820 −8.664 1.141 1.00 38.43 C ATOM 2335 C METC3066 28.641 −3.186 1.340 1.00 37.25 C ATOM 2336 O MET C3066 29.690−2.928 0.753 1.00 37.48 O ATOM 2337 N GLY C3067 27.468 −2.678 0.978 1.0039.12 N ATOM 2338 CA GLY C3067 27.372 −1.782 −0.158 1.00 41.84 C ATOM2339 C GLY C3067 27.338 −2.554 −1.458 1.00 43.68 C ATOM 2340 O GLY C306728.251 −2.446 −2.277 1.00 44.30 O ATOM 2341 N THR C3068 26.281 −3.337−1.648 1.00 45.16 N ATOM 2342 CA THR C3068 26.133 −4.140 −2.853 1.0046.52 C ATOM 2343 CB THR C3068 27.012 −5.409 −2.771 1.00 46.98 C ATOM2344 OG1 THR C3068 26.723 −6.268 −3.880 1.00 47.83 O ATOM 2345 CG2 THRC3068 26.756 −6.154 −1.469 1.00 47.19 C ATOM 2346 C THR C3068 24.679−4.546 −3.076 1.00 47.27 C ATOM 2347 O THR C3068 23.940 −4.800 −2.1231.00 47.53 O ATOM 2348 N GLY C3069 24.272 −4.597 −4.341 1.00 47.97 NATOM 2349 CA GLY C3069 22.908 −4.969 −4.668 1.00 48.41 C ATOM 2350 C GLYC3069 22.848 −6.140 −5.629 1.00 48.94 C ATOM 2351 O GLY C3069 22.349−5.952 −6.758 1.00 49.17 O ATOM 2352 OXT GLY C3069 23.304 −7.244 −5.2571.00 49.26 O TER 2353 GLY C3069 ATOM 2354 C GLY C3074 23.102 −14.343−2.448 1.00 42.87 C ATOM 2355 O GLY C3074 23.918 −14.155 −1.552 1.0043.22 O ATOM 2356 N GLY C3074 23.249 −12.549 −4.163 1.00 43.05 N ATOM2357 CA GLY C3074 23.446 −14.000 −3.885 1.00 42.94 C ATOM 2358 N PHEC3075 21.892 −14.845 −2.228 1.00 42.82 N ATOM 2359 CA PHE C3075 21.441−15.212 −0.890 1.00 42.97 C ATOM 2360 CB PHE C3075 19.920 −15.035 −0.7871.00 43.13 C ATOM 2361 CG PHE C3075 19.484 −13.638 −0.400 1.00 43.82 CATOM 2362 CD1 PHE C3075 20.299 −12.534 −0.647 1.00 43.85 C ATOM 2363 CD2PHE C3075 18.243 −13.429 0.199 1.00 43.74 C ATOM 2364 CE1 PHE C307519.883 −11.243 −0.304 1.00 44.03 C ATOM 2365 CE2 PHE C3075 17.817−12.144 0.545 1.00 44.13 C ATOM 2366 CZ PHE C3075 18.639 −11.049 0.2931.00 44.14 C ATOM 2367 C PHE C3075 21.826 −16.639 −0.516 1.00 42.74 CATOM 2368 O PHE C3075 21.820 −17.007 0.661 1.00 42.92 O ATOM 2369 N GLNC3076 22.175 −17.438 −1.518 1.00 42.00 N ATOM 2370 CA GLN C3076 22.548−18.824 −1.276 1.00 41.00 C ATOM 2371 CB GLN C3076 22.537 −19.615 −2.5871.00 41.57 C ATOM 2372 CG GLN C3076 21.135 −19.865 −3.119 1.00 42.06 CATOM 2373 CD GLN C3076 20.286 −20.695 −2.171 1.00 42.45 C ATOM 2374 OE1GLN C3076 19.056 −20.670 −2.243 1.00 42.81 O ATOM 2375 NE2 GLN C307620.938 −21.445 −1.284 1.00 42.52 N ATOM 2376 C GLN C3076 23.892 −18.977−0.584 1.00 40.27 C ATOM 2377 O GLN C3076 24.216 −20.060 −0.103 1.0040.25 O ATOM 2378 N ASP C3077 24.682 −17.907 −0.537 1.00 38.81 N ATOM2379 CA ASP C3077 25.965 −17.981 0.148 1.00 37.42 C ATOM 2380 CB ASPC3077 27.107 −17.527 −0.769 1.00 39.03 C ATOM 2381 CG ASP C3077 27.008−16.075 −1.152 1.00 40.35 C ATOM 2382 OD1 ASP C3077 25.897 −15.635−1.514 1.00 41.46 O ATOM 2383 OD2 ASP C3077 28.048 −15.379 −1.102 1.0040.89 O ATOM 2384 C ASP C3077 25.926 −17.158 1.438 1.00 35.34 C ATOM2385 O ASP C3077 26.916 −16.556 1.848 1.00 35.66 O ATOM 2386 N LEU C307824.751 −17.142 2.060 1.00 32.99 N ATOM 2387 CA LEU C3078 24.513 −16.4563.328 1.00 30.22 C ATOM 2388 CB LEU C3078 23.775 −15.127 3.113 1.0030.01 C ATOM 2389 CG LEU C3078 24.478 −13.972 2.393 1.00 30.35 C ATOM2390 CD1 LEU C3078 23.555 −12.762 2.352 1.00 29.89 C ATOM 2391 CD2 LEUC3078 25.768 −13.615 3.114 1.00 31.03 C ATOM 2392 C LEU C3078 23.632−17.392 4.165 1.00 27.99 C ATOM 2393 O LEU C3078 22.645 −17.927 3.6591.00 27.40 O ATOM 2394 N GLU C3079 23.984 −17.589 5.435 1.00 25.61 NATOM 2395 CA GLU C3079 23.206 −18.467 6.310 1.00 24.01 C ATOM 2396 CBGLU C3079 23.815 −19.876 6.284 1.00 24.83 C ATOM 2397 CG GLU C307923.137 −20.897 7.190 1.00 25.45 C ATOM 2398 CD GLU C3079 23.716 −22.2907.022 1.00 26.01 C ATOM 2399 OE1 GLU C3079 23.270 −23.022 6.110 1.0026.62 O ATOM 2400 OE2 GLU C3079 24.627 −22.648 7.797 1.00 25.76 O ATOM2401 C GLU C3079 23.113 −17.945 7.756 1.00 22.32 C ATOM 2402 O GLU C307924.113 −17.500 8.335 1.00 21.78 O ATOM 2403 N VAL C3080 21.905 −18.0078.319 1.00 20.99 N ATOM 2404 CA VAL C3080 21.616 −17.554 9.685 1.0019.93 C ATOM 2405 CB VAL C3080 20.634 −16.347 9.666 1.00 19.55 C ATOM2406 CG1 VAL C3080 20.302 −15.911 11.099 1.00 18.41 C ATOM 2407 CG2 VALC3080 21.246 −15.183 8.878 1.00 19.42 C ATOM 2408 C VAL C3080 20.992−18.667 10.550 1.00 20.28 C ATOM 2409 O VAL C3080 19.888 −19.140 10.2611.00 19.70 O ATOM 2410 N LEU C3081 21.701 −19.075 11.606 1.00 20.21 NATOM 2411 CA LEU C3081 21.232 −20.121 12.521 1.00 21.05 C ATOM 2412 CBLEU C3081 22.240 −21.290 12.559 1.00 21.12 C ATOM 2413 CG LEU C308122.698 −21.950 11.246 1.00 20.96 C ATOM 2414 CD1 LEU C3081 23.699−23.067 11.542 1.00 21.74 C ATOM 2415 CD2 LEU C3081 21.497 −22.49810.489 1.00 20.34 C ATOM 2416 C LEU C3081 21.041 −19.566 13.948 1.0021.83 C ATOM 2417 O LEU C3081 21.340 −18.399 14.211 1.00 20.95 O ATOM2418 N ASN C3082 20.546 −20.411 14.855 1.00 22.96 N ATOM 2419 CA ASNC3082 20.322 −20.043 16.262 1.00 24.19 C ATOM 2420 CB ASN C3082 18.857−20.281 16.654 1.00 24.95 C ATOM 2421 CG ASN C3082 17.913 −19.223 16.1011.00 25.21 C ATOM 2422 OD1 ASN C3082 17.843 −18.100 16.611 1.00 26.05 OATOM 2423 ND2 ASN C3082 17.184 −19.577 15.055 1.00 24.39 N ATOM 2424 CASN C3082 21.212 −20.890 17.184 1.00 24.76 C ATOM 2425 O ASN C308221.268 −22.114 17.034 1.00 24.23 O ATOM 2426 N ASN C3083 21.901 −20.25818.133 1.00 24.88 N ATOM 2427 CA ASN C3083 22.753 −21.024 19.046 1.0026.41 C ATOM 2428 CB ASN C3083 23.880 −20.147 19.619 1.00 26.57 C ATOM2429 CG ASN C3083 23.394 −19.088 20.603 1.00 27.00 C ATOM 2430 OD1 ASNC3083 24.185 −18.255 21.047 1.00 28.80 O ATOM 2431 ND2 ASN C3083 22.114−19.115 20.952 1.00 25.26 N ATOM 2432 C ASN C3083 21.922 −21.676 20.1591.00 26.81 C ATOM 2433 O ASN C3083 20.697 −21.536 20.178 1.00 26.49 OATOM 2434 N GLU C3084 22.567 −22.390 21.078 1.00 27.91 N ATOM 2435 CAGLU C3084 21.815 −23.070 22.132 1.00 28.75 C ATOM 2436 CB GLU C308422.716 −24.035 22.917 1.00 29.93 C ATOM 2437 CG GLU C3084 24.064 −23.50623.335 1.00 31.45 C ATOM 2438 CD GLU C3084 24.916 −24.594 23.966 1.0032.85 C ATOM 2439 OE1 GLU C3084 26.051 −24.298 24.397 1.00 33.48 O ATOM2440 OE2 GLU C3084 24.445 −25.752 24.029 1.00 33.46 O ATOM 2441 C GLUC3084 21.024 −22.189 23.092 1.00 28.50 C ATOM 2442 O GLU C3084 20.074−22.664 23.714 1.00 28.13 O ATOM 2443 N ARG C3085 21.399 −20.917 23.2151.00 28.57 N ATOM 2444 CA ARG C3085 20.661 −20.001 24.085 1.00 28.82 CATOM 2445 CB ARG C3085 21.584 −18.929 24.670 1.00 29.93 C ATOM 2446 CGARG C3085 22.566 −19.469 25.692 1.00 31.34 C ATOM 2447 CD ARG C308522.949 −18.409 26.713 1.00 33.11 C ATOM 2448 NE ARG C3085 23.902 −18.93627.683 1.00 33.67 N ATOM 2449 CZ ARG C3085 25.167 −19.217 27.398 1.0034.16 C ATOM 2450 NH1 ARG C3085 25.630 −19.014 26.171 1.00 34.21 N ATOM2451 NH2 ARG C3085 25.965 −19.715 28.330 1.00 33.81 N ATOM 2452 C ARGC3085 19.519 −19.332 23.318 1.00 28.44 C ATOM 2453 O ARG C3085 18.663−18.667 23.912 1.00 28.67 O ATOM 2454 N GLY C3086 19.522 −19.496 21.9961.00 27.15 N ATOM 2455 CA GLY C3086 18.466 −18.928 21.170 1.00 26.89 CATOM 2456 C GLY C3086 18.800 −17.712 20.316 1.00 26.43 C ATOM 2457 O GLYC3086 17.942 −17.229 19.581 1.00 26.94 O ATOM 2458 N ALA C3087 20.031−17.218 20.396 1.00 25.34 N ATOM 2459 CA ALA C3087 20.432 −16.043 19.6221.00 25.00 C ATOM 2460 CB ALA C3087 21.610 −15.361 20.300 1.00 25.01 CATOM 2461 C ALA C3087 20.788 −16.355 18.163 1.00 24.71 C ATOM 2462 O ALAC3087 21.385 −17.394 17.867 1.00 23.78 O ATOM 2463 N PRO C3088 20.413−15.457 17.231 1.00 23.74 N ATOM 2464 CD PRO C3088 19.533 −14.291 17.4481.00 24.91 C ATOM 2465 CA PRO C3088 20.697 −15.631 15.800 1.00 23.12 CATOM 2466 CB PRO C3088 19.628 −14.762 15.136 1.00 24.34 C ATOM 2467 CGPRO C3088 19.551 −13.593 16.083 1.00 24.53 C ATOM 2468 C PRO C308822.115 −15.157 15.466 1.00 22.17 C ATOM 2469 O PRO C3088 22.606 −14.19816.070 1.00 21.42 O ATOM 2470 N TYR C3089 22.765 −15.826 14.512 1.0020.38 N ATOM 2471 CA TYR C3089 24.128 −15.469 14.098 1.00 19.72 C ATOM2472 CB TYR C3089 25.149 −16.054 15.097 1.00 19.67 C ATOM 2473 CG TYRC3089 25.352 −17.564 15.029 1.00 19.93 C ATOM 2474 CD1 TYR C3089 26.410−18.110 14.294 1.00 21.07 C ATOM 2475 CE1 TYR C3089 26.594 −19.49714.194 1.00 20.45 C ATOM 2476 CD2 TYR C3089 24.477 −18.446 15.672 1.0020.53 C ATOM 2477 CE2 TYR C3089 24.653 −19.848 15.578 1.00 20.54 C ATOM2478 CZ TYR C3089 25.717 −20.359 14.833 1.00 20.66 C ATOM 2479 OH TYRC3089 25.908 −21.725 14.713 1.00 19.20 O ATOM 2480 C TYR C3089 24.428−15.972 12.671 1.00 19.17 C ATOM 2481 O TYR C3089 23.820 −16.944 12.2131.00 17.72 O ATOM 2482 N PHE C3090 25.340 −15.295 11.967 1.00 19.73 NATOM 2483 CA PHE C3090 25.729 −15.704 10.607 1.00 20.26 C ATOM 2484 CBPHE C3090 26.310 −14.529 9.800 1.00 20.96 C ATOM 2485 CG PHE C309025.274 −13.607 9.198 1.00 20.15 C ATOM 2486 CD1 PHE C3090 24.812 −12.4999.902 1.00 20.78 C ATOM 2487 CD2 PHE C3090 24.791 −13.831 7.912 1.0020.37 C ATOM 2488 CE1 PHE C3090 23.880 −11.620 9.330 1.00 20.73 C ATOM2489 CE2 PHE C3090 23.860 −12.964 7.326 1.00 20.67 C ATOM 2490 CZ PHEC3090 23.404 −11.853 8.040 1.00 20.35 C ATOM 2491 C PHE C3090 26.788−16.812 10.637 1.00 20.91 C ATOM 2492 O PHE C3090 27.905 −16.598 11.1171.00 20.54 O ATOM 2493 N SER C3091 26.442 −17.986 10.116 1.00 21.82 NATOM 2494 CA SER C3091 27.378 −19.113 10.073 1.00 22.73 C ATOM 2495 CBSER C3091 26.630 −20.435 10.290 1.00 22.96 C ATOM 2496 OG SER C309125.613 −20.617 9.318 1.00 23.28 O ATOM 2497 C SER C3091 28.137 −19.1648.738 1.00 23.33 C ATOM 2498 O SER C3091 29.114 −19.904 8.604 1.00 22.86O ATOM 2499 N GLN C3092 27.683 −18.375 7.762 1.00 23.62 N ATOM 2500 CAGLN C3092 28.309 −18.319 6.436 1.00 24.85 C ATOM 2501 CB GLN C309227.730 −19.439 5.558 1.00 25.88 C ATOM 2502 CG GLN C3092 28.045 −19.3574.064 1.00 28.11 C ATOM 2503 CD GLN C3092 29.529 −19.339 3.762 1.0029.40 C ATOM 2504 OE1 GLN C3092 30.298 −20.131 4.310 1.00 31.43 O ATOM2505 NE2 GLN C3092 29.940 −18.441 2.874 1.00 30.15 N ATOM 2506 C GLNC3092 28.107 −16.944 5.764 1.00 24.73 C ATOM 2507 O GLN C3092 26.974−16.472 5.637 1.00 24.71 O ATOM 2508 N ALA C3093 29.205 −16.310 5.3431.00 23.94 N ATOM 2509 CA ALA C3093 29.160 −14.994 4.685 1.00 23.97 CATOM 2510 CB ALA C3093 28.779 −13.909 5.706 1.00 23.95 C ATOM 2511 C ALAC3093 30.493 −14.618 4.009 1.00 23.83 C ATOM 2512 O ALA C3093 31.556−15.008 4.472 1.00 23.82 O ATOM 2513 N PRO C3094 30.443 −13.841 2.9101.00 24.15 N ATOM 2514 CD PRO C3094 29.221 −13.410 2.203 1.00 24.15 CATOM 2515 CA PRO C3094 31.649 −13.414 2.177 1.00 24.68 C ATOM 2516 CBPRO C3094 31.098 −13.058 0.801 1.00 24.26 C ATOM 2517 CG PRO C309429.762 −12.461 1.144 1.00 24.90 C ATOM 2518 C PRO C3094 32.369 −12.2312.840 1.00 24.92 C ATOM 2519 O PRO C3094 32.529 −11.165 2.239 1.00 25.65O ATOM 2520 N PHE C3095 32.810 −12.437 4.076 1.00 25.08 N ATOM 2521 CAPHE C3095 33.495 −11.410 4.864 1.00 25.37 C ATOM 2522 CB PHE C309532.444 −10.502 5.521 1.00 24.79 C ATOM 2523 CG PHE C3095 33.015 −9.3846.356 1.00 24.93 C ATOM 2524 CD1 PHE C3095 33.652 −8.299 5.760 1.0024.60 C ATOM 2525 CD2 PHE C3095 32.883 −9.403 7.741 1.00 24.43 C ATOM2526 CE1 PHE C3095 34.148 −7.247 6.536 1.00 24.72 C ATOM 2527 CE2 PHEC3095 33.374 −8.358 8.527 1.00 24.22 C ATOM 2528 CZ PHE C3095 34.008−7.278 7.921 1.00 24.70 C ATOM 2529 C PHE C3095 34.288 −12.163 5.9281.00 25.61 C ATOM 2530 O PHE C3095 33.766 −13.101 6.537 1.00 26.06 OATOM 2531 N SER C3096 35.538 −11.773 6.164 1.00 26.42 N ATOM 2532 CA SERC3096 36.343 −12.485 7.158 1.00 27.23 C ATOM 2533 CB SER C3096 37.709−12.857 6.558 1.00 27.32 C ATOM 2534 OG SER C3096 38.389 −11.725 6.0541.00 28.68 O ATOM 2535 C SER C3096 36.529 −11.795 8.515 1.00 27.58 CATOM 2536 O SER C3096 37.311 −12.259 9.349 1.00 28.21 O ATOM 2537 N GLYC3097 35.807 −10.700 8.745 1.00 27.18 N ATOM 2538 CA GLY C3097 35.908−10.003 10.021 1.00 26.33 C ATOM 2539 C GLY C3097 34.808 −10.462 10.9711.00 26.17 C ATOM 2540 O GLY C3097 34.322 −11.584 10.845 1.00 25.72 OATOM 2541 N LYS C3098 34.408 −9.610 11.916 1.00 25.25 N ATOM 2542 CA LYSC3098 33.347 −9.971 12.864 1.00 24.54 C ATOM 2543 CB LYS C3098 33.759−9.591 14.289 1.00 25.96 C ATOM 2544 CG LYS C3098 35.059 −10.259 14.7231.00 28.19 C ATOM 2545 CD LYS C3098 35.079 −10.576 16.208 1.00 29.56 CATOM 2546 CE LYS C3098 35.022 −9.324 17.053 1.00 30.68 C ATOM 2547 NZLYS C3098 35.150 −9.647 18.505 1.00 32.82 N ATOM 2548 C LYS C3098 32.013−9.313 12.498 1.00 22.87 C ATOM 2549 O LYS C3098 31.984 −8.155 12.0821.00 22.97 O ATOM 2550 N ILE C3099 30.919 −10.060 12.659 1.00 21.29 NATOM 2551 CA ILE C3099 29.567 −9.589 12.316 1.00 19.46 C ATOM 2552 CBILE C3099 28.918 −10.546 11.251 1.00 19.44 C ATOM 2553 CG2 ILE C309927.577 −9.987 10.769 1.00 18.38 C ATOM 2554 CG1 ILE C3099 29.869 −10.74210.062 1.00 19.30 C ATOM 2555 CD1 ILE C3099 29.447 −11.853 9.103 1.0019.40 C ATOM 2556 C ILE C3099 28.632 −9.537 13.544 1.00 18.29 C ATOM2557 O ILE C3099 28.381 −10.568 14.165 1.00 18.68 O ATOM 2558 N TRPC3100 28.109 −8.357 13.888 1.00 16.88 N ATOM 2559 CA TRP C3100 27.195−8.233 15.036 1.00 15.59 C ATOM 2560 CB TRP C3100 27.643 −7.078 15.9561.00 15.65 C ATOM 2561 CG TRP C3100 29.076 −7.231 16.505 1.00 15.70 CATOM 2562 CD2 TRP C3100 29.492 −8.034 17.626 1.00 15.13 C ATOM 2563 CE2TRP C3100 30.901 −7.910 17.735 1.00 15.28 C ATOM 2564 CE3 TRP C310028.813 −8.846 18.547 1.00 16.40 C ATOM 2565 CD1 TRP C3100 30.220 −6.66815.997 1.00 15.61 C ATOM 2566 NE1 TRP C3100 31.321 −7.074 16.734 1.0015.83 N ATOM 2567 CZ2 TRP C3100 31.639 −8.570 18.730 1.00 15.21 C ATOM2568 CZ3 TRP C3100 29.549 −9.504 19.538 1.00 15.48 C ATOM 2569 CH2 TRPC3100 30.950 −9.358 19.618 1.00 15.73 C ATOM 2570 C TRP C3100 25.746−8.022 14.533 1.00 15.44 C ATOM 2571 O TRP C3100 25.438 −6.991 13.9241.00 14.84 O ATOM 2572 N LEU C3101 24.875 −9.003 14.800 1.00 14.06 NATOM 2573 CA LEU C3101 23.469 −9.004 14.348 1.00 13.05 C ATOM 2574 CBLEU C3101 23.268 −10.161 13.357 1.00 13.07 C ATOM 2575 CG LEU C310121.828 −10.623 13.084 1.00 12.96 C ATOM 2576 CD1 LEU C3101 21.208 −9.73712.015 1.00 13.42 C ATOM 2577 CD2 LEU C3101 21.821 −12.083 12.624 1.0014.82 C ATOM 2578 C LEU C3101 22.382 −9.133 15.430 1.00 12.57 C ATOM2579 O LEU C3101 22.597 −9.789 16.450 1.00 11.63 O ATOM 2580 N SER C310221.215 −8.525 15.181 1.00 12.95 N ATOM 2581 CA SER C3102 20.054 −8.61516.092 1.00 13.03 C ATOM 2582 CB SER C3102 20.128 −7.536 17.187 1.0013.35 C ATOM 2583 OG SER C3102 19.148 −7.749 18.205 1.00 12.78 O ATOM2584 C SER C3102 18.736 −8.484 15.297 1.00 13.43 C ATOM 2585 O SER C310218.687 −7.747 14.298 1.00 13.38 O ATOM 2586 N ILE C3103 17.687 −9.19715.741 1.00 13.23 N ATOM 2587 CA ILE C3103 16.355 −9.215 15.082 1.0014.65 C ATOM 2588 CB ILE C3103 16.135 −10.552 14.290 1.00 15.02 C ATOM2589 CG2 ILE C3103 14.776 −10.534 13.581 1.00 14.81 C ATOM 2590 CG1 ILEC3103 17.254 −10.764 13.267 1.00 15.40 C ATOM 2591 CD1 ILE C3103 17.113−12.053 12.443 1.00 16.79 C ATOM 2592 C ILE C3103 15.180 −9.123 16.0871.00 15.28 C ATOM 2593 O ILE C3103 15.239 −9.717 17.166 1.00 15.06 OATOM 2594 N SER C3104 14.109 −8.414 15.726 1.00 16.55 N ATOM 2595 CA SERC3104 12.930 −8.295 16.614 1.00 17.82 C ATOM 2596 CB SER C3104 13.077−7.067 17.527 1.00 18.38 C ATOM 2597 OG SER C3104 12.058 −7.028 18.5241.00 18.13 O ATOM 2598 C SER C3104 11.629 −8.186 15.793 1.00 19.18 CATOM 2599 O SER C3104 11.672 −7.850 14.608 1.00 18.60 O ATOM 2600 N HISC3105 10.475 −8.466 16.405 1.00 21.28 N ATOM 2601 CA HIS C3105 9.209−8.376 15.660 1.00 23.07 C ATOM 2602 CB HIS C3105 8.964 −9.664 14.8771.00 24.36 C ATOM 2603 CG HIS C3105 8.715 −10.856 15.749 1.00 25.51 CATOM 2604 CD2 HIS C3105 7.631 −11.219 16.474 1.00 26.93 C ATOM 2605 ND1HIS C3105 9.673 −11.815 15.986 1.00 26.74 N ATOM 2606 CE1 HIS C31059.192 −12.721 16.820 1.00 27.20 C ATOM 2607 NE2 HIS C3105 7.955 −12.38317.132 1.00 28.00 N ATOM 2608 C HIS C3105 7.927 −8.081 16.452 1.00 24.09C ATOM 2609 O HIS C3105 7.913 −8.058 17.686 1.00 23.14 O ATOM 2610 N THRC3106 6.851 −7.870 15.692 1.00 25.15 N ATOM 2611 CA THR C3106 5.506−7.616 16.212 1.00 26.55 C ATOM 2612 CB THR C3106 5.100 −6.137 16.0971.00 26.80 C ATOM 2613 OG1 THR C3106 5.097 −5.748 14.717 1.00 27.05 OATOM 2614 CG2 THR C3106 6.052 −5.258 16.880 1.00 27.26 C ATOM 2615 C THRC3106 4.549 −8.437 15.339 1.00 27.26 C ATOM 2616 O THR C3106 4.987−9.196 14.477 1.00 26.93 O ATOM 2617 N ASP C3107 3.245 −8.287 15.5391.00 28.56 N ATOM 2618 CA ASP C3107 2.310 −9.067 14.732 1.00 30.14 CATOM 2619 CB ASP C3107 0.977 −9.243 15.474 1.00 32.49 C ATOM 2620 CG ASPC3107 0.498 −7.968 16.133 1.00 34.70 C ATOM 2621 OD1 ASP C3107 0.406−6.930 15.440 1.00 37.09 O ATOM 2622 OD2 ASP C3107 0.209 −8.003 17.3481.00 36.52 O ATOM 2623 C ASP C3107 2.065 −8.499 13.334 1.00 29.74 C ATOM2624 O ASP C3107 1.264 −9.043 12.575 1.00 30.83 O ATOM 2625 N GLN C31082.762 −7.425 12.979 1.00 28.55 N ATOM 2626 CA GLN C3108 2.578 −6.81511.665 1.00 27.66 C ATOM 2627 CB GLN C3108 1.942 −5.432 11.822 1.0027.82 C ATOM 2628 CG GLN C3108 0.557 −5.445 12.466 1.00 28.58 C ATOM2629 CD GLN C3108 0.012 −4.045 12.681 0.05 28.18 C ATOM 2630 OE1 GLNC3108 −1.083 −3.866 13.214 0.05 28.21 O ATOM 2631 NE2 GLN C3108 0.779−3.043 12.266 0.05 28.20 N ATOM 2632 C GLN C3108 3.845 −6.693 10.8121.00 26.77 C ATOM 2633 O GLN C3108 3.760 −6.652 9.582 1.00 25.82 O ATOM2634 N PHE C3109 5.015 −6.625 11.449 1.00 25.68 N ATOM 2635 CA PHE C31096.268 −6.496 10.697 1.00 24.08 C ATOM 2636 CB PHE C3109 6.441 −5.03910.221 1.00 25.01 C ATOM 2637 CG PHE C3109 6.572 −4.029 11.343 1.0026.02 C ATOM 2638 CD1 PHE C3109 7.763 −3.908 12.062 1.00 26.89 C ATOM2639 CD2 PHE C3109 5.505 −3.205 11.682 1.00 26.71 C ATOM 2640 CE1 PHEC3109 7.889 −2.977 13.105 1.00 27.26 C ATOM 2641 CE2 PHE C3109 5.616−2.268 12.725 1.00 27.81 C ATOM 2642 CZ PHE C3109 6.811 −2.156 13.4371.00 27.24 C ATOM 2643 C PHE C3109 7.497 −6.950 11.497 1.00 22.66 C ATOM2644 O PHE C3109 7.382 −7.267 12.681 1.00 21.87 O ATOM 2645 N VAL C31108.658 −6.992 10.833 1.00 20.94 N ATOM 2646 CA VAL C3110 9.932 −7.39611.460 1.00 19.58 C ATOM 2647 CB VAL C3110 10.402 −8.790 10.931 1.0020.14 C ATOM 2648 CG1 VAL C3110 10.731 −8.705 9.443 1.00 20.40 C ATOM2649 CG2 VAL C3110 11.639 −9.268 11.707 1.00 21.57 C ATOM 2650 C VALC3110 11.049 −6.374 11.162 1.00 18.29 C ATOM 2651 O VAL C3110 10.982−5.675 10.154 1.00 16.70 O ATOM 2652 N THR C3111 12.065 −6.298 12.0351.00 17.21 N ATOM 2653 CA THR C3111 13.210 −5.383 11.852 1.00 16.21 CATOM 2654 CB THR C3111 13.109 −4.122 12.781 1.00 16.74 C ATOM 2655 OG1THR C3111 13.100 −4.528 14.159 1.00 19.56 O ATOM 2656 CG2 THR C311111.851 −3.321 12.485 1.00 18.23 C ATOM 2657 C THR C3111 14.551 −6.09612.159 1.00 15.10 C ATOM 2658 O THR C3111 14.575 −7.053 12.945 1.0013.98 O ATOM 2659 N ALA C3112 15.643 −5.638 11.532 1.00 13.72 N ATOM2660 CA ALA C3112 16.996 −6.210 11.737 1.00 14.06 C ATOM 2661 CB ALAC3112 17.266 −7.324 10.712 1.00 13.98 C ATOM 2662 C ALA C3112 18.092−5.135 11.630 1.00 13.79 C ATOM 2663 O ALA C3112 17.936 −4.164 10.8841.00 14.41 O ATOM 2664 N SER C3113 19.194 −5.320 12.364 1.00 13.18 NATOM 2665 CA SER C3113 20.321 −4.369 12.395 1.00 12.99 C ATOM 2666 CBSER C3113 20.210 −3.510 13.665 1.00 12.64 C ATOM 2667 OG SER C311321.209 −2.499 13.724 1.00 12.28 O ATOM 2668 C SER C3113 21.690 −5.10312.369 1.00 13.25 C ATOM 2669 O SER C3113 21.875 −6.075 13.097 1.0012.44 O ATOM 2670 N VAL C3114 22.636 −4.611 11.555 1.00 13.63 N ATOM2671 CA VAL C3114 23.972 −5.230 11.374 1.00 13.14 C ATOM 2672 CB VALC3114 24.030 −5.984 9.989 1.00 12.86 C ATOM 2673 CG1 VAL C3114 25.467−6.425 9.641 1.00 13.59 C ATOM 2674 CG2 VAL C3114 23.117 −7.194 10.0161.00 13.11 C ATOM 2675 C VAL C3114 25.161 −4.248 11.419 1.00 13.18 CATOM 2676 O VAL C3114 25.094 −3.171 10.834 1.00 11.64 O ATOM 2677 N ILEC3115 26.245 −4.631 12.101 1.00 14.05 N ATOM 2678 CA ILE C3115 27.463−3.797 12.176 1.00 15.16 C ATOM 2679 CB ILE C3115 27.717 −3.208 13.5931.00 15.92 C ATOM 2680 CG2 ILE C3115 28.902 −2.217 13.532 1.00 16.68 CATOM 2681 CG1 ILE C3115 26.482 −2.477 14.122 1.00 15.85 C ATOM 2682 CD1ILE C3115 26.657 −1.949 15.549 1.00 15.56 C ATOM 2683 C ILE C3115 28.699−4.655 11.836 1.00 16.02 C ATOM 2684 O ILE C3115 28.900 −5.714 12.4441.00 14.67 O ATOM 2685 N LEU C3116 29.519 −4.195 10.883 1.00 16.42 NATOM 2686 CA LEU C3116 30.741 −4.920 10.469 1.00 17.73 C ATOM 2687 CBLEU C3116 30.864 −4.910 8.939 1.00 17.22 C ATOM 2688 CG LEU C3116 29.646−5.423 8.157 1.00 17.27 C ATOM 2689 CD1 LEU C3116 29.914 −5.349 6.6601.00 17.70 C ATOM 2690 CD2 LEU C3116 29.339 −6.855 8.570 1.00 18.07 CATOM 2691 C LEU C3116 32.016 −4.322 11.099 1.00 18.48 C ATOM 2692 O LEUC3116 32.185 −3.101 11.134 1.00 16.07 O ATOM 2693 N GLU C3117 32.926−5.184 11.562 1.00 20.56 N ATOM 2694 CA GLU C3117 34.150 −4.718 12.2271.00 23.53 C ATOM 2695 CB GLU C3117 33.939 −4.757 13.754 1.00 24.06 CATOM 2696 CG GLU C3117 35.200 −4.587 14.608 1.00 24.76 C ATOM 2697 CDGLU C3117 34.952 −4.835 16.103 1.00 25.52 C ATOM 2698 OE1 GLU C311734.507 −5.946 16.473 1.00 25.65 O ATOM 2699 OE2 GLU C3117 35.203 −3.91716.913 1.00 25.88 O ATOM 2700 C GLU C3117 35.429 −5.488 11.878 1.0025.38 C ATOM 2701 O GLU C3117 35.403 −6.695 11.654 1.00 25.28 O ATOM2702 N GLU C3118 36.545 −4.766 11.840 1.00 28.60 N ATOM 2703 CA GLUC3118 37.857 −5.346 11.559 1.00 32.23 C ATOM 2704 CB GLU C3118 38.321−4.996 10.139 1.00 33.43 C ATOM 2705 CG GLU C3118 37.520 −5.678 9.0381.00 35.47 C ATOM 2706 CD GLU C3118 38.123 −5.482 7.657 1.00 36.73 CATOM 2707 OE1 GLU C3118 37.561 −6.029 6.683 1.00 37.62 O ATOM 2708 OE2GLU C3118 39.156 −4.786 7.540 1.00 37.51 O ATOM 2709 C GLU C3118 38.857−4.800 12.576 1.00 33.91 C ATOM 2710 O GLU C3118 39.168 −3.608 12.5761.00 34.12 O ATOM 2711 N ASN C3119 39.348 −5.678 13.444 1.00 36.07 NATOM 2712 CA ASN C3119 40.308 −5.298 14.477 1.00 37.92 C ATOM 2713 CBASN C3119 40.307 −6.343 15.597 1.00 38.97 C ATOM 2714 CG ASN C311938.908 −6.622 16.137 1.00 39.98 C ATOM 2715 OD1 ASN C3119 38.271 −5.75316.737 1.00 40.51 O ATOM 2716 ND2 ASN C3119 38.424 −7.841 15.919 1.0040.65 N ATOM 2717 C ASN C3119 41.713 −5.169 13.889 1.00 38.71 C ATOM2718 O ASN C3119 41.850 −5.354 12.662 1.00 39.38 O ATOM 2719 OXT ASNC3119 42.661 −4.885 14.657 1.00 39.94 O TER 2720 ASN C3119 ATOM 2721 OHOH W5001 1.203 5.537 8.026 1.00 17.73 O ATOM 2722 O HOH W5002 14.8159.909 2.322 1.00 14.32 O ATOM 2723 O HOH W5003 23.904 8.622 37.957 1.0027.02 O ATOM 2724 O HOH W5004 20.469 3.444 3.735 1.00 17.55 O ATOM 2725O HOH W5005 24.018 4.203 28.855 1.00 20.10 O ATOM 2726 O HOH W500610.973 5.376 28.684 1.00 19.79 O ATOM 2727 O HOH W5007 22.784 15.31434.546 1.00 22.90 O ATOM 2728 O HOH W5008 23.453 4.929 3.777 1.00 19.63O ATOM 2729 O HOH W5009 23.062 1.129 4.843 1.00 21.68 O ATOM 2730 O HOHW5010 25.642 18.163 37.608 1.00 19.94 O ATOM 2731 O HOH W5011 23.1842.653 2.606 1.00 26.65 O ATOM 2732 O HOH W5012 28.019 0.947 5.252 1.0022.66 O ATOM 2733 O HOH W5013 4.711 21.958 2.912 1.00 24.85 O ATOM 2734O HOH W5014 36.483 3.458 10.706 1.00 31.97 O ATOM 2735 O HOH W501517.241 0.177 14.610 1.00 23.93 O ATOM 2736 O HOH W5016 13.566 −15.29611.672 1.00 22.95 O ATOM 2737 O HOH W5017 19.479 14.186 −2.520 1.0025.49 O ATOM 2738 O HOH W5018 27.283 10.084 6.422 1.00 24.49 O ATOM 2739O HOH W5019 14.135 8.932 34.920 1.00 26.53 O ATOM 2740 O HOH W502036.044 2.408 16.583 1.00 32.56 O ATOM 2741 O HOH W5021 33.258 −17.3633.678 1.00 19.73 O ATOM 2742 O HOH W5022 15.667 −0.884 2.725 1.00 31.95O ATOM 2743 O HOH W5023 9.740 −0.876 42.696 1.00 26.45 O ATOM 2744 O HOHW5024 28.298 −24.311 26.736 1.00 36.28 O ATOM 2745 O HOH W5025 16.1702.461 13.853 1.00 22.79 O ATOM 2746 O HOH W5026 13.623 −1.972 15.9221.00 33.10 O ATOM 2747 O HOH W5027 35.568 −7.137 18.918 1.00 28.33 OATOM 2748 O HOH W5028 21.193 8.337 22.471 1.00 24.39 O ATOM 2749 O HOHW5029 0.905 8.530 3.669 1.00 29.99 O ATOM 2750 O HOH W5030 26.791 21.66430.504 1.00 26.91 O ATOM 2751 O HOH W5031 12.687 −4.279 3.191 1.00 33.49O ATOM 2752 O HOH W5032 25.981 5.485 38.408 1.00 30.01 O ATOM 2753 O HOHW5033 18.351 −22.326 27.170 1.00 39.62 O ATOM 2754 O HOH W5034 27.692−22.175 28.942 1.00 33.59 O ATOM 2755 O HOH W5035 7.766 9.184 29.1491.00 37.38 O ATOM 2756 O HOH W5036 27.081 7.365 5.947 1.00 37.77 O ATOM2757 O HOH W5037 26.538 19.381 35.080 1.00 37.77 O ATOM 2758 O HOH W5038−4.201 17.799 6.607 1.00 32.96 O ATOM 2759 O HOH W5039 5.036 8.70014.260 1.00 30.11 O ATOM 2760 O HOH W5040 0.851 9.642 42.538 1.00 22.98O ATOM 2761 O HOH W5041 19.927 0.231 15.198 1.00 20.70 O ATOM 2762 O HOHW5042 38.613 −9.206 13.685 1.00 46.18 O ATOM 2763 O HOH W5043 35.672−15.638 5.122 1.00 43.16 O ATOM 2764 O HOH W5044 14.774 −8.966 39.5621.00 27.43 O ATOM 2765 O HOH W5045 −0.343 −11.294 8.886 1.00 35.83 OATOM 2766 O HOH W5046 0.384 7.133 40.132 1.00 36.11 O ATOM 2767 O HOHW5047 −1.790 −16.597 10.364 1.00 51.74 O ATOM 2768 O HOH W5048 17.9138.434 22.684 1.00 19.14 O ATOM 2769 O HOH W5049 26.849 7.812 30.849 1.0032.50 O ATOM 2770 O HOH W5050 31.682 10.495 7.280 1.00 43.96 O ATOM 2771O HOH W5051 33.295 7.550 31.842 1.00 42.65 O ATOM 2772 O HOH W505226.726 22.667 9.308 1.00 42.17 O ATOM 2773 O HOH W5053 16.839 2.65343.220 1.00 32.73 O ATOM 2774 O HOH W5054 28.300 3.705 0.074 1.00 31.84O ATOM 2775 O HOH W5055 21.249 10.241 40.281 1.00 40.01 O ATOM 2776 OHOH W5056 18.910 0.164 43.189 1.00 35.91 O ATOM 2777 O HOH W5057 14.29325.027 1.495 1.00 30.20 O ATOM 2778 O HOH W5058 15.432 −0.416 17.5181.00 26.65 O ATOM 2779 O HOH W5059 21.028 5.383 41.219 1.00 31.60 O ATOM2780 O HOH W5060 27.025 7.703 33.714 1.00 38.38 O ATOM 2781 O HOH W50611.162 −2.470 38.136 1.00 32.76 O ATOM 2782 O HOH W5062 7.118 −4.4683.111 1.00 25.42 O ATOM 2783 O HOH W5063 10.345 8.046 50.558 1.00 21.47O ATOM 2784 O HOH W5064 1.601 −6.957 7.392 1.00 19.01 O ATOM 2785 O HOHW5065 8.301 8.667 48.256 1.00 31.31 O ATOM 2786 O HOH W5066 13.857 7.1521.988 1.00 29.65 O ATOM 2787 O HOH W5067 −8.101 −4.494 44.898 1.00 34.47O ATOM 2788 O HOH W5068 31.896 −17.405 6.589 1.00 41.64 O ATOM 2789 OHOH W5069 17.654 −25.606 27.581 1.00 27.36 O ATOM 2790 O HOH W507023.222 14.650 26.416 1.00 26.05 O ATOM 2791 O HOH W5071 7.588 −0.5280.314 1.00 32.42 O ATOM 2792 O HOH W5072 37.956 −17.275 4.444 1.00 27.98O ATOM 2793 O HOH W5073 13.506 −13.814 28.837 1.00 53.93 O ATOM 2794 OHOH W5074 32.339 6.763 6.234 1.00 44.01 O ATOM 2795 O HOH W5075 17.732−21.822 12.391 1.00 27.13 O ATOM 2796 O HOH W5076 2.962 14.623 32.9431.00 35.34 O ATOM 2797 O HOH W5077 18.219 −11.144 17.921 1.00 32.13 OATOM 2798 O HOH W5078 21.073 24.057 −0.096 1.00 34.29 O ATOM 2799 O HOHW5079 15.379 −12.595 24.369 1.00 37.81 O ATOM 2800 O HOH W5080 26.13121.190 0.182 1.00 31.04 O ATOM 2801 O HOH W5081 −7.427 −1.162 30.1531.00 37.22 O ATOM 2802 O HOH W5082 9.376 19.648 13.353 1.00 46.89 O ATOM2803 O HOH W5083 26.771 −14.783 26.158 1.00 30.66 O ATOM 2804 O HOHW5085 24.158 −4.023 38.598 1.00 29.95 O ATOM 2805 O HOH W5086 2.673−2.236 40.838 1.00 36.71 O ATOM 2806 O HOH W5087 14.901 15.719 31.7931.00 66.05 O ATOM 2807 O HOH W5089 0.185 6.149 5.302 1.00 45.92 O ATOM2808 O HOH W5090 −3.050 13.963 3.439 1.00 31.57 O ATOM 2809 O HOH W509120.002 26.238 4.307 1.00 38.95 O ATOM 2810 O HOH W5092 9.528 7.01025.049 1.00 40.00 O ATOM 2811 O HOH W5093 22.998 9.245 25.495 1.00 45.96O ATOM 2812 O HOH W5094 25.633 5.504 41.203 1.00 33.74 O ATOM 2813 O HOHW5095 22.525 7.413 40.125 1.00 27.93 O ATOM 2814 O HOH W5096 25.772−0.812 38.637 1.00 43.16 O ATOM 2815 O HOH W5097 1.675 3.923 15.398 1.0024.93 O ATOM 2816 O HOH W5098 3.426 25.166 2.688 1.00 33.60 O ATOM 2817O HOH W5099 6.716 24.079 2.431 1.00 30.61 O ATOM 2818 O HOH W5100 13.7762.826 15.316 1.00 35.09 O ATOM 2819 O HOH W5101 2.840 22.627 5.321 1.0028.88 O ATOM 2820 O HOH W5102 4.306 26.695 0.803 1.00 45.75 O ATOM 2821O HOH W5103 28.312 3.533 30.225 1.00 30.56 O ATOM 2822 O HOH W5104 7.2965.105 45.493 1.00 44.55 O ATOM 2823 O HOH W5105 8.727 −7.822 20.152 1.0030.96 O ATOM 2824 O HOH W5106 15.910 2.991 1.288 1.00 26.19 O ATOM 2825O HOH W5107 24.692 15.648 32.485 1.00 45.46 O ATOM 2826 O HOH W510810.229 10.752 16.032 1.00 39.52 O ATOM 2827 O HOH W5109 30.124 8.4921.194 1.00 42.53 O ATOM 2828 O HOH W5110 38.431 9.460 12.406 1.00 34.79O ATOM 2829 O HOH W5111 15.296 −0.704 44.230 1.00 30.31 O ATOM 2830 OHOH W5112 22.219 −25.058 0.518 1.00 40.16 O ATOM 2831 O HOH W5113 16.280−1.757 13.031 1.00 32.98 O ATOM 2832 O HOH W5114 7.672 5.118 50.500 1.0042.44 O ATOM 2833 O HOH W5116 19.588 26.165 1.692 1.00 35.11 O ATOM 2834O HOH W5117 29.689 0.468 33.170 1.00 50.63 O ATOM 2835 O HOH W511827.638 14.621 27.167 1.00 37.33 O ATOM 2836 O HOH W5119 25.674 24.1226.832 1.00 44.26 O ATOM 2837 O HOH W5120 40.801 −13.288 5.322 1.00 31.98O ATOM 2838 O HOH W5121 36.143 −1.829 16.148 1.00 41.24 O ATOM 2839 OHOH W5122 3.151 5.682 48.883 1.00 34.36 O ATOM 2840 O HOH W5123 32.69314.445 9.290 1.00 34.74 O ATOM 2841 O HOH W5124 28.701 6.185 34.708 1.0049.77 O ATOM 2842 O HOH W5125 26.196 1.517 −1.280 1.00 39.43 O ATOM 2843O HOH W5126 −0.033 0.726 10.398 1.00 47.62 O ATOM 2844 O HOH W512721.383 −3.597 −1.922 1.00 51.56 O ATOM 2845 O HOH W5128 13.364 12.83327.633 1.00 52.29 O ATOM 2846 O HOH W5129 21.714 12.615 35.721 1.0033.09 O ATOM 2847 O HOH W5130 8.469 6.895 52.440 1.00 45.76 O ATOM 2848O HOH W5131 26.110 4.660 30.832 1.00 35.30 O ATOM 2849 O HOH W513219.463 −23.363 14.165 1.00 35.76 O ATOM 2850 O HOH W5133 13.443 20.073−9.252 1.00 40.04 O ATOM 2851 O HOH W5134 9.131 8.743 16.901 1.00 44.35O ATOM 2852 O HOH W5135 2.141 8.144 15.984 1.00 43.82 O ATOM 2853 O HOHW5136 8.533 27.824 6.026 1.00 33.71 O ATOM 2854 O HOH W5137 23.48923.402 0.284 1.00 47.94 O ATOM 2855 O HOH W5138 19.996 15.564 −7.4511.00 42.23 O ATOM 2856 O HOH W5139 3.830 6.820 −6.454 1.00 43.70 O ATOM2857 O HOH W5140 15.282 15.611 18.402 1.00 41.11 O ATOM 2858 O HOH W514117.265 26.061 11.713 1.00 39.14 O ATOM 2859 O HOH W5142 23.754 1.893−2.493 1.00 45.81 O ATOM 2860 O HOH W5143 26.488 3.338 6.608 1.00 42.72O ATOM 2861 O HOH W5144 6.963 4.729 1.634 1.00 33.11 O ATOM 2862 O HOHW5145 −0.293 3.358 3.517 1.00 47.82 O ATOM 2863 O HOH W5146 13.304 0.01014.071 1.00 44.49 O ATOM 2864 O HOH W5147 14.485 −0.911 11.196 1.0034.10 O ATOM 2865 O HOH W5148 38.684 −3.391 16.424 1.00 42.58 O ATOM2866 O HOH W5149 −0.378 −3.887 41.179 1.00 39.92 O ATOM 2867 O HOH W515014.999 10.060 38.087 1.00 56.40 O ATOM 2868 O HOH W5151 27.440 −10.39433.773 1.00 51.57 O ATOM 2869 O HOH W5152 9.035 −7.425 0.106 1.00 46.37O ATOM 2870 O HOH W5153 5.110 −2.372 2.316 1.00 33.68 O ATOM 2871 O HOHW5154 29.018 −14.387 13.400 1.00 40.14 O ATOM 2872 O HOH W5155 1.676−2.447 9.577 1.00 41.85 O ATOM 2873 O HOH W5156 20.185 11.538 −6.6351.00 37.49 O ATOM 2874 O HOH W5157 15.389 −28.857 26.962 1.00 41.90 OATOM 2875 O HOH W5158 −6.106 19.784 6.635 1.00 36.72 O ATOM 2876 O HOHW5159 5.517 17.184 13.233 1.00 48.23 O ATOM 2877 O HOH W5160 5.07615.020 11.985 1.00 45.45 O ATOM 2878 O HOH W5161 5.445 −7.849 27.6591.00 39.11 O ATOM 2879 O HOH W5162 20.980 18.101 37.922 1.00 29.42 OATOM 2880 O HOH W5163 16.748 −29.146 3.293 1.00 42.39 O ATOM 2881 O HOHW5164 30.770 4.871 31.188 1.00 43.36 O ATOM 2882 O HOH W5165 3.854−8.929 29.337 1.00 54.81 O ATOM 2883 O HOH W5166 10.593 19.605 16.0421.00 47.04 O ATOM 2884 O HOH W5167 42.095 8.840 19.150 1.00 49.61 O ATOM2885 O HOH W5168 9.957 11.390 13.550 1.00 42.37 O ATOM 2886 O HOH W5169−4.606 21.333 1.399 1.00 48.40 O ATOM 2887 O HOH W5170 11.695 29.3426.480 1.00 58.15 O ATOM 2888 O HOH W5171 23.099 25.128 3.657 1.00 40.99O ATOM 2889 O HOH W5172 23.505 24.766 −3.702 1.00 44.31 O ATOM 2890 OHOH W5173 14.447 17.461 20.573 1.00 40.93 O ATOM 2891 O HOH W5174 11.97423.606 15.698 1.00 50.59 O ATOM 2892 O HOH W5175 33.868 19.345 11.3741.00 39.71 O ATOM 2893 O HOH W5176 8.306 −9.142 31.222 1.00 42.33 O ATOM2894 O HOH W5177 12.171 14.379 29.266 1.00 52.75 O ATOM 2895 O HOH W517829.974 −2.958 37.157 1.00 38.64 O ATOM 2896 O HOH W5179 30.177 1.1023.621 1.00 43.39 O ATOM 2897 O HOH W5180 13.634 0.062 1.980 1.00 43.54 OATOM 2898 O HOH W5181 9.893 10.792 25.719 1.00 35.63 O ATOM 2899 O HOHW5182 15.133 16.851 24.775 1.00 34.15 O TER 2900 HOH W5182 ATOM 2901 N1ACOE E4002 19.788 −13.382 22.863 1.00 37.66 N ATOM 2902 C2A COE E400219.629 −12.509 21.832 1.00 37.59 C ATOM 2903 N3A COE E4002 18.590−12.603 20.980 1.00 37.39 N ATOM 2904 C4A COE E4002 17.686 −13.62721.196 1.00 37.85 C ATOM 2905 C5A COE E4002 17.805 −14.571 22.262 1.0038.04 C ATOM 2906 C6A COE E4002 18.900 −14.393 23.079 1.00 38.11 C ATOM2907 N6A COE E4002 19.128 −15.221 24.120 1.00 38.32 N ATOM 2908 N7A COEE4002 16.749 −15.454 22.198 1.00 38.10 N ATOM 2909 C8A COE E4002 15.977−15.090 21.125 1.00 38.02 C ATOM 2910 N9A COE E4002 16.529 −13.99020.508 1.00 38.30 N ATOM 2911 C71 COE E4002 15.927 −13.354 19.309 1.0038.56 C ATOM 2912 C72 COE E4002 15.686 −14.244 18.059 1.00 38.64 C ATOM2913 O72 COE E4002 16.358 −13.703 16.916 1.00 37.72 O ATOM 2914 C73 COEE4002 14.168 −14.225 17.883 1.00 39.06 C ATOM 2915 O73 COE E4002 13.797−14.451 16.455 1.00 38.84 O ATOM 2916 P73 COE E4002 14.041 −15.82215.721 1.00 39.24 P ATOM 2917 O7A COE E4002 13.165 −15.826 14.433 1.0039.04 O ATOM 2918 O8A COE E4002 15.540 −15.939 15.325 1.00 39.12 O ATOM2919 O9A COE E4002 13.637 −17.009 16.646 1.00 39.35 O ATOM 2920 C74 COEE4002 13.826 −12.831 18.392 1.00 39.77 C ATOM 2921 O74 COE E4002 14.690−12.631 19.516 1.00 39.23 O ATOM 2922 C75 COE E4002 12.345 −12.65718.817 1.00 40.70 C ATOM 2923 O75 COE E4002 12.121 −11.261 19.226 1.0042.75 O ATOM 2924 P1A COE E4002 10.787 −10.752 19.901 1.00 43.64 P ATOM2925 O3A COE E4002 9.754 −11.915 20.051 1.00 43.83 O ATOM 2926 O4A COEE4002 10.208 −9.595 19.036 1.00 44.05 O ATOM 2927 O5A COE E4002 11.200−10.230 21.306 1.00 43.87 O TER 2928 COE E4002 END

[0364]

1 6 1 122 PRT Streptococcus pneumoniae mat_peptide (1)..() 1 Met Arg MetIle Val Gly His Gly Ile Asp Ile Glu Glu Leu Ala Ser 1 5 10 15 Ile GluSer Ala Val Thr Arg His Glu Gly Phe Ala Lys Arg Val Leu 20 25 30 Thr AlaGln Glu Met Glu Arg Phe Thr Ser Leu Lys Gly Arg Arg Gln 35 40 45 Ile GluTyr Leu Ala Gly Arg Trp Ser Ala Lys Glu Ala Phe Ser Lys 50 55 60 Ala MetGly Thr Gly Ile Ser Lys Leu Gly Phe Gln Asp Leu Glu Val 65 70 75 80 LeuAsn Asn Glu Arg Gly Ala Pro Tyr Phe Ser Gln Ala Pro Phe Ser 85 90 95 GlyLys Ile Trp Leu Ser Ile Ser His Thr Asp Gln Phe Val Thr Ala 100 105 110Ser Val Ile Leu Glu Glu Asn His Glu Ser 115 120 2 34 DNA ArtificialSequence PCR Primer 2 cgcggatccc atatgatagt tggacacgga attg 34 3 31 DNAArtificial Sequence PCR Primer 3 cgcggatccc tagctttcat gaatttcctc c 31 443 DNA Artificial Sequence PCR Primer 4 cgcggatccc atatgacaga aaaagaaatttttgaccgta ttg 43 5 45 DNA Artificial Sequence PCR Primer 5 cgcggatccgaattcctatt ttccttgaat gattttaacc acatc 45 6 9 PRT Streptococcuspneumoniae 6 Met Ile Val Gly His Gly Ile Asp Ile 1 5

What is claimed is:
 1. A composition, comprising a crystal of isolatedStreptococcus pneumoniae acyl carrier protein synthase.
 2. Thecomposition of claim 1, wherein said crystal effectively diffractsX-rays, and permits the determination of the atomic coordinates of saidacyl carrier protein synthase to a resolution of about 2.0 Å.
 3. Thecomposition of claim 1, wherein said Streptococcus pneumoniae acylcarrier protein synthase has an active site cavity comprising the3′,5′-adenosine diphosphate binding site shown in FIG.
 9. 4. Thecomposition of claim 1, wherein said Streptococcus pneumoniae acylcarrier protein synthase is a homotrimer, wherein each protomercomprises the following structural motifs: (a) a three-strandedanti-parallel β-sheet formed by strands β1, β5, and β4; (b) a longα-helix that packs diagonally against said β-sheet, together withα-helices α1, α2, α3, and α4 of an anti-parallel four helical bundle;and (c) a long, extended loop with a two-strand anti-parallel β-sheetcomprising strands β2 and β3, wherein said structural motifs (a), (b),and (c) are organized such that said long helix α4 runs through saidhomotrimer, and is surrounded by the remainder of said structuralmotifs, as shown in FIGS. 8(B) and 8(C).
 5. The composition of claim 1,wherein said crystal belongs to orthorhombic space group P2₁2₁2₁, withunit cell dimensions of a=49.8 Å, b=59.6 Å, and c=114.7 Å, or monoclinicspace group C2, with unit cell dimensions of a=120.2 Å, b=62.3 Å, c=51.7Å, and β=98.7°.
 6. The composition of claim 1, wherein said acyl carrierprotein synthase comprises selenocysteine or selenomethionine.
 7. Thecomposition of claim 1, wherein said acyl carrier protein synthasecomprises a heavy metal atom.
 8. The composition of claim 1, furthercomprising a chemical compound complexed covalently or non-covalentlywith said crystal.
 9. The composition of claim 8, wherein said chemicalcompound is 3′,5′-adenosine diphosphate.
 10. The composition claim 9,wherein said crystal belongs to monoclinic space group C2, with unitcell dimensions of a=120.2 Å, b=62.3 Å, c=51.7 Å, and β=98.7°.
 11. Thecomposition of claim 1, wherein said Streptococcus pneumoniae acylcarrier protein synthase has the amino acid sequence shown in SEQ IDNO:1.
 12. The composition of claim 1, wherein said crystal has theatomic coordinates shown in Table 3 or Table
 4. 13. The composition ofclaim 9, wherein said crystal has the atomic coordinates shown in Table5.
 14. A composition, comprising a crystal of Streptococcus pneumoniaeacyl carrier protein synthase having the amino acid sequence shown inSEQ ID NO: 1 wherein methionine is substituted with selenomethioinine,wherein said acyl carrier protein synthase is a homotrimer, wherein eachprotomer comprises the following structural motifs: (d) a three-strandedanti-parallel β-sheet formed by strands β1, β5, and β4; (e) a longα-helix that packs diagonally against said β-sheet, together withα-helices α1, α2, α3, and α4 of an anti-parallel four helical bundle;and (f) a long, extended loop with a two-strand anti-parallel β-sheetcomprising strands β2 and β3, wherein said structural motifs (a), (b),and (c) are organized such that said long helix α4 runs through saidhomotrimer, and is surrounded by the remainder of said structuralmotifs, as shown in FIGS. 8(B) and 8(C); wherein when said acyl carrierprotein synthase is in native form, said crystal belongs to orthorhombicspace group P2₁2₁2₁, with unit cell dimensions of a=49.8 Å, b=59.6 Å,and c=114.7 Å, or monoclinic space group C2, with unit cell dimensionsof a=120.2 Å, b=62.3 Å, c=51.7 Å, and β=98.7°, and wherein said crystalhas the atomic coordinates shown in Table 3 or Table 4, respectively;and wherein when said acyl carrier protein synthase is complexed with3′,5′-adenosine diphosphate, said crystal belongs to monoclinic spacegroup C2, with unit cell dimensions of a=120.2 Å, b=62.3 Å, c=51.7 Å,and β=98.7°, and wherein said crystal has the atomic coordinates shownin Table
 5. 15. An enzyme active site crystal structure comprising the3′,5′-adenosine diphosphate binding site shown in FIG.
 9. 16. The enzymeactive site crystal structure of claim 15, wherein said enzyme comprisesisolated, properly folded Streptococcus pneumoniae acyl carrier proteinsynthase, or a fragment thereof comprising said active site.
 17. Amethod of isolating Streptococcus pneumoniae acyl carrier proteinsynthase, comprising: (a) growing said Streptococcus pneumoniae in amedium lacking methionine but containing L-selenomethionine; (b)preparing a cell extract of said Streptococcus pneumoniae; (c)centrifuging said cell extract to produce a supernatant fraction, andcollecting said supernatant fraction; (d) chromatographing saidsupernatant fraction on a cation exchange column in buffer containingdithiothreitol or β-mercaptoethanol, and collecting fractions containingsaid Streptococcus pneumoniae acyl carrier protein synthase; (e)chromatographing said fractions of step (d) on a gel filtration columnin buffer containing dithiothreitol or β-mercaptoethanol, and collectingfractions containing said Streptococcus pneumoniae acyl carrier proteinsynthase comprising L-selenomethionine.
 18. The method of claim 17,further comprising chromatographing said fractions of step (e) on ananion exchange column in buffer containing dithiothreitol orβ-mercaptoethanol, and collecting fractions containing saidStreptococcus pneumoniae acyl carrier protein synthase.
 19. The methodof claim 18, wherein said Streptococcus pneumoniae acyl carrier proteinsynthase has the amino acid sequence shown in SEQ ID NO:1, whereinmethionine is replaced with L-selenomethionine.
 20. IsolatedStreptococcus pneumoniae acyl carrier protein synthase produced by themethod of claim
 19. 21. A method of producing a crystal of Streptococcuspneumoniae acyl carrier protein synthase that diffracts X-rays,comprising: (a) providing Streptococcus pneumoniae acyl carrier proteinsynthase isolated according to claim 19; (b) concentrating said acylcarrier protein synthase to 8 mg/ml in a solution containing 10 mMMgCl₂, 14 mM KCl, and 20 mM Tris-HCl at pH
 7. 1 to produce aconcentrated protein solution; (c) equilibrating a 4 μl drop of saidacyl carrier protein synthase in a solution comprising a mixture of 1:1, v/v, concentrated protein solution as in step (b)/reservoir solutionover a 500 μL reservoir solution comprising 8-15% polyethyleneglycol4000, 200 mM ammonium sulfate, and 100 mM citrate buffer at pH
 4. 5; and(d) growing a crystal of said acyl carrier protein synthase by vapordiffusion at 294K for at least 4 to 5 days.
 22. The method of claim 21,further comprising determining a three-dimensional structure of saidcrystal.
 23. The method of claim 21, wherein said crystal belongs toorthorhombic space group P2₁2₁2₁, having unit cell parameters a=49.8 Å,b=59.6 Å, c=114.7 Å, or monoclinic space group C2, having unit cellparameters a=120.2 Å, b=62.3 Å, c=51.7 Å, β=98.7°), comprises onehomotrimeric molecule per asymmetric unit, and has the atomiccoordinates shown in Table 3 or Table
 4. 24. The method of claim 21,further comprising testing the ability of a compound to form a complexwith an active site of said acyl carrier protein synthase by includingsaid compound in said concentrated protein solution of step (b).
 25. Themethod of claim 21, further comprising contacting said crystal of acylcarrier protein synthase and a solution comprising a compound ofinterest to form a mixture, incubating said mixture to permit saidcompound to diffuse into said crystal, and determining whether saidcompound forms a complex with said acyl carrier protein synthase. 26.The method of claim 25, wherein said compound is 3′,5′-adenosinediphosphate.
 27. The method of claim 25, wherein when said compoundforms a complex with said acyl carrier protein synthase, determining athree-dimensional structure of said acyl carrier proteinsynthaselcompound crystal complex.
 28. The method of claim 26, whereinsaid crystal belongs to monoclinic space group C2, having unit cellparameters a=120.2 Å, b=62.3 Å, c=51.7 Å, β=98.7°, comprises onehomotrimeric molecule per asymmetric unit, and has the atomiccoordinates shown in Table
 5. 29. A crystal of Streptococcus pneumoniaeacyl carrier protein synthase produced by the method of claim
 21. 30. Acrystal of Streptococcus pneumoniae acyl carrier protein synthaseproduced by the method of claim
 24. 31. A crystal of Streptococcuspneumoniae acyl carrier protein synthase produced by the method of claim25.